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Escherichia coli K-12 substr. MG1655 Protein: DNA polymerase III, holoenzyme

Subunit composition of DNA polymerase III, holoenzyme = [(DnaE)(DnaQ)(HolE)]3[(DnaX)3(HolB)(HolA)][(DnaN)2]2[(DnaX)2][(HolC)(HolD)]4
         DNA polymerase III, core enzyme = (DnaE)(DnaQ)(HolE) (summary available)
                 DNA polymerase III, α subunit = DnaE (extended summary available)
                 DNA polymerase III, ε subunit = DnaQ (extended summary available)
                 DNA polymerase III, θ subunit = HolE (extended summary available)
         DNA polymerase III, preinitiation complex = (DnaX)3(HolB)(HolA) (extended summary available)
                 DNA polymerase III, τ subunit = DnaX
                 DNA polymerase III, δ prime subunit = HolB (summary available)
                 DNA polymerase III, δ subunit = HolA (summary available)
         DNA polymerase III, β subunit = (DnaN)2 (extended summary available)
         DNA polymerase III, τ subunit dimer = (DnaX)2 (extended summary available)
                 DNA polymerase III, τ subunit = DnaX
         DNA polymerase III, ψ-χ subunit = (HolC)(HolD) (extended summary available)
                 DNA polymerase III, χ subunit = HolC
                 DNA polymerase III, ψ subunit = HolD

Summary:
DNA polymerase III holoenzyme is the enzyme primarily responsible for replicative DNA synthesis in E. coli. It carries out primer-initiated 5' to 3' polymerization of DNA on a single-stranded DNA template, as well as 3' to 5' exonucleolytic editing of mispaired nucleotides.

Replicative DNA polymerization begins when the preinitiation complex binds single-stranded DNA near an RNA primer. The preinitiation complex then loads the beta processivity clamp onto the DNA at this site, after which three core polymerases, chaperoned into place by the tau subunit, bind to the processivity clamp, with one polymerase on the leading strand and two on the lagging. DNA is synthesized 5' to 3' from primers on both the leading and lagging strands, covalently attaching the newly synthesized DNA to the primer. Tau displaces beta in the presence of duplex DNA, dissociating the polymerase from the template when it reaches a temporary stop on the lagging strand or when synthesis is complete on either strand [Maki88, Maki88a, Onrust95, Maki88b, Nusslein76, ReyesLamothe10].

For more detailed discussion of the stages of polymerase binding and DNA synthesis, see the individual entries for DNA polymerase III, preinitiation complex, DNA polymerase III, β subunit, DNA polymerase III, τ subunit dimer, DNA polymerase III, core enzyme and their constituent parts.

DNA polymerase III binds a region about 30 nucleotides long upstream of the RNA primer, with the alpha subunit making contact 9 nucleotides upstream and the beta clamp making contact 22 nucleotides upstream [Reems95, Reems94]. The preinitiation complex binds an area larger than this prior to being displaced by the core polymerase [Reems94]. In the presence of DNA polymerase III, RNA primer length is limited to 10 nucleotides, a limitation that is independent of the epsilon-mediated 3' to 5' exonuclease activity [Zechner92].

During polymerization, DNA polymerase III pauses at sites of potential secondary structure [LaDuca83]. The holoenzyme can traverse distances as long as 400 base pairs of duplex DNA to reach the next available 3' end and restart synthesis [ODonnell85]. Such jumps within the same template take 2 to 5 seconds, whereas transfer to a new template takes 30 seconds [Burgers83].

DNA polymerase III is required for several kinds of DNA repair, including some forms of double-strand break repair, fixing hydrogen-peroxide-induced damage and methyl-directed mismatch repair [Motamedi99, Hagensee89, Cooper93]. Mutations that inhibit polymerase III stimulate repeat expansion and lead to lower levels of unsaturation in fatty acids [Morag99, Suzuki98b].

UV mutagenesis and gap repair following UV damage to DNA both involve DNA polymerase III [CohenFix94, Tomer96]. The polymerase stalls at pyrimidine photodimers in vitro, but is capable of bypassing such lesions to continue synthesis [Shwartz87, Livneh86]. This bypass activity is stimulated by single-strand binding protein (SSB) but inhibited by the polymerase III beta subunit, which explains the relatively low rate of bypass in vivo [Shwartz87, Shavitt89].

Citations: [Cull95]

Gene-Reaction Schematic: ?

Credits:
Last-Curated ? 09-Jan-2006 by Shearer A , SRI International


Subunit of DNA polymerase III, holoenzyme: DNA polymerase III, core enzyme

Locations: cytosol

GO Terms:

Cellular Component: GO:0005829 - cytosol

Summary:
The DNA polymerase III core enzyme contains one each of the alpha, epsilon and theta subunits and can carry out the basic polymerase and exonuclease activities of polymerase III [McHenry79].

Based on yeast two-hybrid data, both alpha and theta interact with epsilon, but not each other [Jonczyk98]. The interaction between epsilon and theta has been examined via lanthanide-labeling NMR [Pintacuda06]. In a cell-free translation system, theta is required for the generation of soluble epsilon. An NMR analysis of cell-free DNA core enzyme shows epsilon connects to alpha via a flexible linker region [Ozawa08].


Component enzyme of DNA polymerase III, core enzyme : DNA polymerase III, α subunit

Synonyms: SdgC, PolC, DnaE

Gene: dnaE Accession Numbers: EG10238 (EcoCyc), b0184, ECK0183

Locations: cytosol

Sequence Length: 1160 AAs

Molecular Weight: 129.9 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis Inferred from experiment [Maki85, UniProtGOA11a, GOA01a, GOA01]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0003887 - DNA-directed DNA polymerase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01, Maki85]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Toste13, Jergic13, Kelman98, Kim96d, Rajagopala12, Stukenberg91, Ozawa08, Gao01a, Butland05, Jonczyk98, Oishi06]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Maki85]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9458N , EcoliWiki:b0184 , Mint:MINT-1224103 , ModBase:P10443 , PR:PRO_000022462 , Pride:P10443 , Protein Model Portal:P10443 , RefSeq:NP_414726 , SMR:P10443 , String:511145.b0184 , UniProt:P10443

Relationship Links: InterPro:IN-FAMILY:IPR003141 , InterPro:IN-FAMILY:IPR004013 , InterPro:IN-FAMILY:IPR004365 , InterPro:IN-FAMILY:IPR004805 , InterPro:IN-FAMILY:IPR011708 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR016195 , PDB:Structure:2HNH , PDB:Structure:2HQA , PDB:Structure:4GX8 , PDB:Structure:4GX9 , PDB:Structure:4JOM , Pfam:IN-FAMILY:PF01336 , Pfam:IN-FAMILY:PF02811 , Pfam:IN-FAMILY:PF07733 , Smart:IN-FAMILY:SM00481

Catalyzes:
a deoxyribonucleoside triphosphate + (deoxynucleotides)(n) = (deoxynucleotides)(n+1) + diphosphate

Summary:
The alpha subunit of DNA polymerase III catalyzes the polymerase activity of the holoenzyme complex [Maki85]. Replicative 5' to 3' polymerization of DNA requires dNTPs and template DNA with a bound RNA primer [Kornberg72, Hurwitz74]. The newly polymerized DNA is covalently attached to the RNA primer [Livingston75]. The presence of the epsilon subunit increases the polymerase activity of the alpha subunit two-fold [Maki87].

The alpha subunit is required for misincorporation and bypass during UV mutagenesis [Sharif90, Bridges90].

The middle portion of the alpha subunit (residues 542-991) is involved in binding to the polymerase III beta subunit. Deletion of the amino-terminal portion of alpha (residues 1-542) actually increases its affinity for beta [Kim96e]. The carboxy-terminus of alpha is required for binding to the polymerase III tau subunit [Kim96d]. The amino-terminal php domain of alpha is required for binding to the epsilon subunit [Wieczorek06].

Transcription of dnaE is induced by nalidixic acid, but not by mitomycin C, and induction does not require LexA [Van01a].

Overproduction of alpha can compensate for an otherwise lethal deficiency in DNA polymerase I [Witkin92].

A crystal structure of the first 917 amino acids of DnaE has been determined to 2.3 Å resolution [Lamers06].

Citations: [Welch82]

Essentiality data for dnaE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Component enzyme of DNA polymerase III, core enzyme : DNA polymerase III, ε subunit

Synonyms: MutD, DnaQ

Gene: dnaQ Accession Numbers: EG10243 (EcoCyc), b0215, ECK0215

Locations: cytosol

Sequence Length: 243 AAs

Molecular Weight: 27.099 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0045004 - DNA replication proofreading Inferred from experiment [Echols83]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis Inferred from experiment [Scheuermann84, UniProtGOA11a, GOA01]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0004527 - exonuclease activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Scheuermann84]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Toste13, Jergic13, Hamdan02, Kelman98, Stukenberg91, Ozawa08, Butland05, Jonczyk98, Oishi06]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0004518 - nuclease activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication
information transfer protein related chaperoning, repair (refolding)

Unification Links: DIP:DIP-9462N , EcoliWiki:b0215 , Mint:MINT-1222832 , ModBase:P03007 , PR:PRO_000022467 , Protein Model Portal:P03007 , RefSeq:NP_414751 , SMR:P03007 , String:511145.b0215 , UniProt:P03007

Relationship Links: InterPro:IN-FAMILY:IPR006054 , InterPro:IN-FAMILY:IPR006055 , InterPro:IN-FAMILY:IPR006309 , InterPro:IN-FAMILY:IPR012337 , InterPro:IN-FAMILY:IPR013520 , PDB:Structure:1J53 , PDB:Structure:1J54 , PDB:Structure:1MGZ , PDB:Structure:2GUI , PDB:Structure:2IDO , PDB:Structure:2XY8 , PDB:Structure:4GX8 , PDB:Structure:4GX9 , Pfam:IN-FAMILY:PF00929 , Smart:IN-FAMILY:SM00479

Catalyzes:
DNAn + n H2O → n a nucleoside 5'-monophosphate

Summary:
The epsilon subunit of DNA polymerase III catalyzes the 3' to 5' proofreading exonuclease activity of the holoenzyme [Echols83, Livingston75a, Scheuermann84]. This activity is required to prevent spontaneous mutations and may play a role in preventing UV mutagenesis and lesion bypass synthesis as well [Woodgate87, Ciesla90, Pages05]. The epsilon subunit suppresses both misincorporation of dCMP and transversion mutations [Maki90, Wu90]. Episilon isrequired for speed and processivity of DNA polymerase III function [Studwell90].

In the presence of polymerase III alpha subunit, epsilon activity increases ten- to eighty-fold, and its affinity for the 3'-hydroxy terminus of DNA increases substantially [Maki87]. Single-stranded DNA binding protein inhibits epsilon activity during replication [Shwartz88].

The structure of epsilon complexed with a bacteriophage homolog of theta has been determined to 2.1 Å [Kirby06].

dnaQ is induced following exposure to various mutagenic and DNA-damaging substances, often in an SOS-response-dependent manner [Quinones90, Quinones89, Kaasch89, Quinones88].

In a dnaQ mutant, CAG and CTG trinucleotide repeats are destabilized and lose their orientation dependence. This effect appears to require SbcCD ATP-dependent dsDNA exonuclease [Zahra07].

Citations: [Scheuermann83, DiFrancesco84]

Essentiality data for dnaQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of DNA polymerase III, core enzyme: DNA polymerase III, θ subunit

Synonyms: HolE

Gene: holE Accession Numbers: EG11505 (EcoCyc), b1842, ECK1843

Locations: cytosol

Sequence Length: 76 AAs

Molecular Weight: 8.846 kD (from nucleotide sequence)

Molecular Weight: 10.0 kD (experimental) [McHenry79]

GO Terms:

Biological Process: GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Hamdan02, Ozawa08, Jonczyk98, Butland05, Oishi06]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]
GO:0005737 - cytoplasm

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-39982N , EcoliWiki:b1842 , Mint:MINT-1223798 , ModBase:P0ABS8 , PR:PRO_000022920 , Pride:P0ABS8 , Protein Model Portal:P0ABS8 , RefSeq:NP_416356 , SMR:P0ABS8 , String:511145.b1842 , UniProt:P0ABS8

Relationship Links: InterPro:IN-FAMILY:IPR009052 , InterPro:IN-FAMILY:IPR011325 , PDB:Structure:1DU2 , PDB:Structure:2AE9 , PDB:Structure:2AXD , PDB:Structure:2XY8 , Pfam:IN-FAMILY:PF06440 , ProDom:IN-FAMILY:PD057609

Summary:
The theta subunit of DNA polymerase III (HolE) binds tightly to the epsilon subunit but not to the alpha subunit [StudwellVaughan93]. This binding appears to enhance interaction between alpha and epsilon as well as slightly stimulating epsilon proofreading activity [TaftBenz04, StudwellVaughan93]. Loss of theta yields no significant growth phenotype, and theta does not appear to be required for speed or processivity of DNA polymerase III holoenzyme [Slater94, Studwell90]. Theta may enhance the stability of epsilon [Conte12].

HolE may have a "moonlighting" function in the cell. Both YdgT and HolE appear to influence expression of tnaA by enhancing transcription termination at the leader DNA sequence [Dietrich13].

Based on an NMR characterization, the surface of theta is bipolar, with the positive and negative charges grouped at opposite ends of the protein [Keniry00]. It also appears to have exposed hydrophobic residues [Mueller05]. A solution structure of the theta in a complex with the N-terminal domain of epsilon has been solved [Keniry06].

A holE deletion strain appears to contain a lower amount of unassociated epsilon subunit [Conte12]. Microarray analysis of a holE mutant showed altered expression of a set of genes that overlapped significantly with genes whose expression was changed in a ydgT mutant [Dietrich13].

Citations: [Kim96f, Jonczyk98, Li99d, DeRose03, Gupta04, Ozawa08, Ozawa13]

Essentiality data for holE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of DNA polymerase III, holoenzyme: DNA polymerase III, preinitiation complex

Summary:
The preinitiation complex binds primed ssDNA and loads the beta processivity clamp. Following this, the DNA polymerase III (pol III) core enzyme, linked by tau, binds, allowing processive DNA polymerization [ODonnell87].

Several of the preinitiation complex subunits are required for binding and initiation of replication. The delta subunit interacts with the primer-template junction, ensuring proper placement of the preinitiation complex at a replication start site [Magdalena04]. The complex binds single-strand binding protein (SSB)-coated DNA with the assistance of associated psi-chi dimers [Fradkin92, Glover98]. The interaction with SSB bound to DNA is a thousand-fold stronger than that with SSB alone; it also enhances the affinity of SSB for DNA, preventing premature dissociation from the initiation site [Glover98, Witte03].

Beta clamps are loaded onto DNA by the preinitiation complex. Contact between the complex and beta is primarily mediated by delta, which can bind to the beta carboxy-termini and remove the beta clamp from DNA in an ATP-independent manner [Leu00, Naktinis95, Indiani03]. Free delta is also present in the cell, possibly acting to remove beta clamps from DNA where no polymerase is present [Leu00]. Preinitiation complex binding to beta does require ATP, suggesting a possible conformational change to reveal delta [Naktinis95]. The delta and delta' subunits themselves undergo only minor conformational changes on ATP binding [Goedken04]. The gamma subunit can also open the beta clamp, though less effectively than delta [Leu01]. Both gamma and delta' restrict opening of beta by delta in the absence of ATP [Leu01]. The preinitiation complex loads beta onto template DNA at a rate of 12/s, which is fast enough to account for the rate of lagging strand initiation [Bloom96].

Beta loading and preinitiation complex release from DNA are both ATP-dependent processes. Each gamma subunit binds an ATP, prompting a conformational change that induces delta' to permit delta to bind and act on the beta clamp [Hingorani98, Turner99]. ATP binding also raises the affinity of the preinitiation complex for primed template [Ason00]. This same primed template triggers hydrolysis of bound ATP, possibly via the interaction between beta and primed DNA, reverting the complex to a lower affinity form that cycles off the DNA and disengages from beta [Ason03, Turner99, Bertram98]. The involvement of ATP and its hydrolysis in beta loading and subsequent preinitiation complex release has been examined in detail [Hingorani99, Bertram00, Snyder04, Williams04].

A number of structural studies have been carried out on the preinitiation complex, sometimes with conflicting results. In addition to the 2 gamma, 1 delta, 1 delta', 1 chi, 1 psi structure found in the holoenzyme, a tau variant with tau, delta, delta', chi and psi can form in vitro [Onrust95, Onrust95a]. In sedimentation assays, gamma and tau have both been detected as homotetramers both on their own and complexed with delta, delta', chi and psi [Dallmann95]. Within the preinitiation complex, gamma crosslinks with both delta' and psi [Glover00]. A crystal structure of the entire complex at 2.7 A resolution shows a pentameric arrangement of subunits including three gamma subunits [Jeruzalmi01]. Another crystal structure, of delta and beta together, shows that delta operates to open beta by perturbing one of the beta dimer interface points [Jeruzalmi01a].


Subunit of DNA polymerase III, preinitiation complex: DNA polymerase III, τ subunit

Synonyms: DnaZ, DnaX, DNA elongation factor III

Gene: dnaX Accession Numbers: EG10245 (EcoCyc), b0470, ECK0464

Sequence Length: 643 AAs

Molecular Weight: 71.138 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred from experiment [Tsuchihashi89]
GO:0006260 - DNA replication Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Henson79]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Kelman98, Kim96d, Naktinis95, Olson95, Rajagopala12, Parks09, Simonetta09, Butland05, Kazmirski04, Bullard02, Song01a, Jeruzalmi01, Glover01, Pritchard00, Gao01b, Gao01a, Gao01c]
GO:0016887 - ATPase activity Inferred from experiment [Tsuchihashi89]
GO:0017111 - nucleoside-triphosphatase activity Inferred from experiment [Walker00]
GO:0030337 - DNA polymerase processivity factor activity Inferred from experiment [Olson95, Jeruzalmi01]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Glover01]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0043846 - DNA polymerase III, clamp loader complex Inferred from experiment [Blinkova93]
GO:0009360 - DNA polymerase III complex Inferred by computational analysis [GOA01]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9464N , EcoliWiki:b0470 , Mint:MINT-1222776 , ModBase:P06710 , PR:PRO_000022469 , Pride:P06710 , Protein Model Portal:P06710 , RefSeq:NP_415003 , SMR:P06710 , String:511145.b0470 , UniProt:P06710

Relationship Links: InterPro:IN-FAMILY:IPR001270 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR008921 , InterPro:IN-FAMILY:IPR012763 , InterPro:IN-FAMILY:IPR021029 , InterPro:IN-FAMILY:IPR022001 , InterPro:IN-FAMILY:IPR022754 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1JR3 , PDB:Structure:1NJF , PDB:Structure:1NJG , PDB:Structure:1XXH , PDB:Structure:1XXI , PDB:Structure:2AYA , PDB:Structure:3GLF , PDB:Structure:3GLG , PDB:Structure:3GLH , PDB:Structure:3GLI , Pfam:IN-FAMILY:PF12168 , Pfam:IN-FAMILY:PF12169 , Pfam:IN-FAMILY:PF12170 , Prints:IN-FAMILY:PR00300 , Smart:IN-FAMILY:SM00382

Essentiality data for dnaX knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of DNA polymerase III, preinitiation complex: DNA polymerase III, δ prime subunit

Synonyms: HolB

Gene: holB Accession Numbers: EG11500 (EcoCyc), b1099, ECK1085

Locations: cytosol

Sequence Length: 334 AAs

Molecular Weight: 36.937 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006261 - DNA-dependent DNA replication Inferred from experiment [Magdalena04]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Kelman98, Olson95, Simonetta09, Butland05, Kazmirski04, Bullard02, Song01a, Jeruzalmi01, Song01b, Glover01, Pritchard00, Gao01c, Li08b]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01, Magdalena04]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0008408 - 3'-5' exonuclease activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009360 - DNA polymerase III complex Inferred from experiment Inferred by computational analysis [GOA01, Naktinis95]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9932N , EcoliWiki:b1099 , Mint:MINT-1239429 , ModBase:P28631 , PR:PRO_000022917 , Protein Model Portal:P28631 , RefSeq:NP_415617 , SMR:P28631 , String:511145.b1099 , UniProt:P28631

Relationship Links: InterPro:IN-FAMILY:IPR004622 , InterPro:IN-FAMILY:IPR008921 , InterPro:IN-FAMILY:IPR015199 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1A5T , PDB:Structure:1JR3 , PDB:Structure:1XXH , PDB:Structure:1XXI , PDB:Structure:3GLF , PDB:Structure:3GLG , PDB:Structure:3GLH , PDB:Structure:3GLI , Pfam:IN-FAMILY:PF09115

Summary:
The crystal structure of delta' has been determined. It is composed of three domains arranged in a "C" shape, with a nonfunctional nucleotide binding site in its amino-terminus [Guenther97].

Citations: [Dong93c, Carter93]

Essentiality data for holB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of DNA polymerase III, preinitiation complex: DNA polymerase III, δ subunit

Synonyms: HolA

Gene: holA Accession Numbers: EG11412 (EcoCyc), b0640, ECK0633

Locations: cytosol

Sequence Length: 343 AAs

Molecular Weight: 38.704 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006261 - DNA-dependent DNA replication Inferred from experiment [Leu00]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Kelman98, Rajagopala14, Naktinis95, Olson95, Butland05, Bullard02, Song01a, Song01b, Pritchard00, Parks09, Li08b, Jeruzalmi01a]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009360 - DNA polymerase III complex Inferred from experiment Inferred by computational analysis [GOA01, Naktinis95]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9931N , EcoliWiki:b0640 , Mint:MINT-1235044 , ModBase:P28630 , PR:PRO_000022916 , Protein Model Portal:P28630 , RefSeq:NP_415173 , SMR:P28630 , String:511145.b0640 , UniProt:P28630

Relationship Links: InterPro:IN-FAMILY:IPR005790 , InterPro:IN-FAMILY:IPR008921 , InterPro:IN-FAMILY:IPR010372 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1JQJ , PDB:Structure:1JQL , PDB:Structure:1JR3 , PDB:Structure:1XXH , PDB:Structure:1XXI , PDB:Structure:3GLF , PDB:Structure:3GLG , PDB:Structure:3GLH , PDB:Structure:3GLI , Pfam:IN-FAMILY:PF06144

Summary:
Some delta exists independent of the preinitiation complex, possibly playing a role in stripping beta clamps from DNA in the absence of replication initiation [Leu00].The preinitiation complex binds primed ssDNA and loads the beta processivity clamp. Following this, the DNA polymerase III (pol III) core enzyme, linked by tau, binds, allowing processive DNA polymerization [ODonnell87].

Citations: [Dong93c]

Essentiality data for holA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of DNA polymerase III, holoenzyme: DNA polymerase III, β subunit

Gene: dnaN Accession Numbers: EG10242 (EcoCyc), b3701, ECK3693

Locations: cytosol

Subunit composition of DNA polymerase III, β subunit = [DnaN]2

Map Position: [3,879,244 <- 3,880,344] (83.61 centisomes)
Length: 1101 bp / 366 aa

Molecular Weight of Polypeptide: 40.587 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006271 - DNA strand elongation involved in DNA replication Inferred from experiment [LaDuca86]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Toste13, Jergic13, Bunting03, Kurz04, Kelman98, Naktinis95, Keyamura11, Stukenberg91, Parks09, Butland05, Jeruzalmi01a]
GO:0042802 - identical protein binding Inferred from experiment [Hauser14, Rajagopala14, Jergic13, Kong92, Lasserre06, Rajagopala09]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0008408 - 3'-5' exonuclease activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009360 - DNA polymerase III complex Inferred by computational analysis [GOA01]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-36038N , EcoliWiki:b3701 , ModBase:P0A988 , PR:PRO_000022466 , Pride:P0A988 , Protein Model Portal:P0A988 , RefSeq:NP_418156 , SMR:P0A988 , String:511145.b3701 , UniProt:P0A988

Relationship Links: InterPro:IN-FAMILY:IPR001001 , InterPro:IN-FAMILY:IPR022634 , InterPro:IN-FAMILY:IPR022635 , InterPro:IN-FAMILY:IPR022637 , PDB:Structure:1JQJ , PDB:Structure:1JQL , PDB:Structure:1MMI , PDB:Structure:1OK7 , PDB:Structure:1UNN , PDB:Structure:1WAI , PDB:Structure:2POL , PDB:Structure:2XUR , PDB:Structure:3BEP , PDB:Structure:3D1E , PDB:Structure:3D1F , PDB:Structure:3D1G , PDB:Structure:3F1V , PDB:Structure:3PWE , PDB:Structure:3Q4J , PDB:Structure:3Q4K , PDB:Structure:3Q4L , PDB:Structure:3QSB , PDB:Structure:4K3K , PDB:Structure:4K3L , PDB:Structure:4K3M , PDB:Structure:4K3O , PDB:Structure:4K3P , PDB:Structure:4K3Q , PDB:Structure:4K3R , PDB:Structure:4K3S , PDB:Structure:4MJP , PDB:Structure:4MJQ , PDB:Structure:4MJR , Pfam:IN-FAMILY:PF00712 , Pfam:IN-FAMILY:PF02767 , Pfam:IN-FAMILY:PF02768 , Smart:IN-FAMILY:SM00480

Summary:
The beta subunit of DNA polymerase III dimerizes to form the sliding clamp that links the core polymerase to DNA and allows processive DNA replication.

Beta binds 3' to an RNA primer at an ssDNA/duplex DNA junction in an ATP-dependent process catalyzed by the preinitiation complex [Maki88, Yao00]. The presence of beta stimulates DNA polymerase III activity, resulting in increased product length and processivity [LaDuca86]. The complete DNA polymerase III holoenzyme with both beta and ATP is at least twenty times more processive than core enzyme or holoenzyme lacking either of those components [Burgers82].

The beta clamp is very stable on DNA, requiring the ATP-dependent action of DNA polymerase III delta subunit for removal [Leu00]. Divalent magnesium is required for beta to maintain its dimer structure [Griep88]. On its own, the beta dimer diffuses bidirectionally on DNA in an ATP-independent fashion [Stukenberg91].

Beta binds to the core polymerase via the seven carboxy-terminal residues of the alpha subunit [Stukenberg91, Burnouf04]. Alpha interacts with the same portion of beta as the preinitiation protein delta, displacing delta and the preinitiation complex when it binds. Other polymerases (I, II, IV, V) also bind there as well [Lopez03]. Polymerase IV and the polymerase III core enzyme have been shown to compete for binding to beta [Burnouf04]. Beta is required for polymerase V-dependent translesion synthesis, but this uses a different interaction surface on beta than polymerase III [Sutton05]. Many proteins that bind beta have the consensus beta-binding motif QL(S/D)LF [Wijffels04].

A number of beta crystal structures have been evaluated. Based on a structure at 2.5 Å resolution, the beta dimer forms a ring with twelve internal α-helices, and each beta monomer has three identical domains [Kong92]. Crystal structures have also been determined at 1.9 and 1.85 A resolution [Oakley03]. A crystal structure of the interaction between beta and polymerase IV has also been determined [Burnouf04].

Beta is induced in an SOS-dependent manner following UV irradiation and exposure to an alkylating agent [Quinones89, Quillardet03]. Induction following UV exposure is posttranscriptional [Tadmor94]. UV irradiation has also been shown to induce synthesis of beta*, an in-frame isoform of beta that forms a homotrimer, can stimulate polymerase III activity and increases UV resistance [Skaliter96, PazElizur96, Skaliter96a]. Beta is also induced on entrance to stationary phase [Villarroya98].

The position of beta in the cell has been tracked. Beta exists in one or two condensed clusters in the nucleoid during normal growth and moves to the cell poles during replication [Onogi02].

dnaN has been the subject of a pilot study to screen for genetic interactions with null alleles in the Keio collection [Yong13].

Citations: [Burgers81, Johanson80]

Gene Citations: [PerezRoger91, Macian94]

Essentiality data for dnaN knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of DNA polymerase III, holoenzyme: DNA polymerase III, τ subunit dimer

Synonyms: dnaZ, DNA elongation factor III

Gene: dnaX Accession Numbers: EG10245 (EcoCyc), b0470, ECK0464

Subunit composition of DNA polymerase III, τ subunit dimer = [DnaX]2
         DNA polymerase III, τ subunit = DnaX

Map Position: [491,316 -> 493,247] (10.59 centisomes)
Length: 1932 bp / 643 aa

Molecular Weight of Polypeptide: 71.138 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred from experiment [Tsuchihashi89]
GO:0006260 - DNA replication Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Henson79]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Kelman98, Kim96d, Naktinis95, Olson95, Rajagopala12, Parks09, Simonetta09, Butland05, Kazmirski04, Bullard02, Song01a, Jeruzalmi01, Glover01, Pritchard00, Gao01b, Gao01a, Gao01c]
GO:0016887 - ATPase activity Inferred from experiment [Tsuchihashi89]
GO:0017111 - nucleoside-triphosphatase activity Inferred from experiment [Walker00]
GO:0030337 - DNA polymerase processivity factor activity Inferred from experiment [Olson95, Jeruzalmi01]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Glover01]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0043846 - DNA polymerase III, clamp loader complex Inferred from experiment [Blinkova93]
GO:0009360 - DNA polymerase III complex Inferred by computational analysis [GOA01]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9464N , EcoliWiki:b0470 , Mint:MINT-1222776 , ModBase:P06710 , PR:PRO_000022469 , Pride:P06710 , Protein Model Portal:P06710 , RefSeq:NP_415003 , SMR:P06710 , String:511145.b0470 , UniProt:P06710

Relationship Links: InterPro:IN-FAMILY:IPR001270 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR008921 , InterPro:IN-FAMILY:IPR012763 , InterPro:IN-FAMILY:IPR021029 , InterPro:IN-FAMILY:IPR022001 , InterPro:IN-FAMILY:IPR022754 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1JR3 , PDB:Structure:1NJF , PDB:Structure:1NJG , PDB:Structure:1XXH , PDB:Structure:1XXI , PDB:Structure:2AYA , PDB:Structure:3GLF , PDB:Structure:3GLG , PDB:Structure:3GLH , PDB:Structure:3GLI , Pfam:IN-FAMILY:PF12168 , Pfam:IN-FAMILY:PF12169 , Pfam:IN-FAMILY:PF12170 , Prints:IN-FAMILY:PR00300 , Smart:IN-FAMILY:SM00382

Summary:
As described in the gamma subunit description, DnaX undergoes a programmed -1 frameshift roughly half of the time that yields a new stop codon just after the frameshift point [Tsuchihashi90, Flower90, Blinkowa90].

The "Spliced Nucleotide Sequence" link above refers to this frameshifted variant, but note that no splicing occurs.
The tau subunit of DNA polymerase III holoenzyme binds the alpha subunit and dimerizes, dimerizing the core alpha-epsilon-theta polymerase as a consequence [StudwellVaughan91]. This dimerization of the core polymerase is required for processive lagging strand synthesis [Kim96g]. Alpha binds within the tau carboxy-terminus [StudwellVaughan91, Gao01a]. Tau interacts with alpha at the beta binding site with high affinity in the presence of duplex DNA and low affinity in the presence of primed ssDNA. As a consequence, when synthesis is complete tau blocks beta binding, leading to release of polymerase from the beta clamp [Lopez03a].

Tau also binds the replicative DNA helicase DnaB. This requires the fourth of five domains in tau, and leads to binding of the hexameric DnaB by more than one tau, suggesting both taus in the polymerase III holoenzyme are bound [Gao01b, Dallmann00]. This interaction is required to allow DNA synthesis to proceed at its normal rate of one thousand nucleotides per second. Without this interaction, DNA polymerase III moves at the rate of DnaB alone, about thirty-five nucleotides per second [Kim96h].

In the absence of tau, leading-strand synthesis by DNA polymerase III is not highly processive and requires an excess of core enzyme [Kim96i, Dallmann95a].

Tau also has an ssDNA-dependent ATpase activity, as well as DNA-DNA and DNA-RNA annealing activities that do not require ATP binding or hydrolysis [Lee87, Kim95c]. Based on the annealing activities, a role for tau in primer stabilization has been suggested [Kim95c].

Tau shares the first three of its five domains with the gamma subunit. The third domain is required for oligomerization of both tau and gamma, and also includes the binding sites for delta, delta', chi and psi [Glover01, Gao01c].

Gene Citations: [Chen93c]

Essentiality data for dnaX knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of DNA polymerase III, holoenzyme: DNA polymerase III, ψ-χ subunit

Summary:
The ψ-χ dimer is an accessory protein that significantly enhances the ability of the DNA polymerase III preiniation complex to bind template DNA and initiate replication.

ψ-χ acts in multiple ways to improve polymerase binding and subsequent activity. The dimer interacts directly with single-strand binding protein (SSB) via binding to the carboxy-terminus of SSB [Glover98, Witte03, Kelman98]. This increases the overall affinity of the preinitiation complex for SSB-bound template [Glover98]. The interaction between the ψ subunit of ψ-χ and the preinitation complex also stabilizes the high-DNA-affinity, post-ATP state of the preinitiation complex, helping maintain the complex's affinity for template DNA [Anderson07]. Finally, the binding of the χ subunit to SSB disrupts the SSB-primase interaction, aiding release of primase from the primer, thus paving the way for the initiation of replication [Yuzhakov99].

ψ-χ interacts with the preinitiation complex via binding of the ψ amino-terminus to the complex. A 3.5 Å structure of the isolated ψ amino-terminus bound to this complex suggests tight binding [Simonetta09].

The structure of the ψ-χ dimer has been crystallized to 2.1 Å resolution [Olson95, Gulbis04, Xiao93a].


Subunit of DNA polymerase III, ψ-χ subunit: DNA polymerase III, χ subunit

Synonyms: HolC

Gene: holC Accession Numbers: EG11413 (EcoCyc), b4259, ECK4252

Locations: cytosol

Sequence Length: 147 AAs

Molecular Weight: 16.633 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0032298 - positive regulation of DNA-dependent DNA replication initiation Inferred from experiment [Yuzhakov99]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Naktinis95, Rajagopala14, Glover01, Gao01c, Yuzhakov99, Kelman98, Marceau11, Kozlov10, Xiao93a, Olson95, Rajagopala12, Song01a, Butland05, Gulbis04]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0043847 - DNA polymerase III, clamp loader chi/psi subcomplex Inferred from experiment [Glover98, Witte03]
GO:0005737 - cytoplasm
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9933N , EcoliWiki:b4259 , Mint:MINT-1224072 , ModBase:P28905 , PR:PRO_000022918 , Protein Model Portal:P28905 , RefSeq:NP_418680 , SMR:P28905 , String:511145.b4259 , UniProt:P28905

Relationship Links: InterPro:IN-FAMILY:IPR007459 , PDB:Structure:1EM8 , PDB:Structure:3SXU , Pfam:IN-FAMILY:PF04364

Citations: [Carter93a, Xiao93b]

Essentiality data for holC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of DNA polymerase III, ψ-χ subunit: DNA polymerase III, ψ subunit

Synonyms: HolD

Gene: holD Accession Numbers: EG11414 (EcoCyc), b4372, ECK4363

Locations: cytosol

Sequence Length: 137 AAs

Molecular Weight: 15.174 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Marceau11, Kelman98, Xiao93a, Naktinis95, Olson95, Rajagopala12, Simonetta09, Song01a, Glover01, Gao01c, Butland05, Gulbis04]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, GOA01]
GO:0008408 - 3'-5' exonuclease activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9934N , EcoliWiki:b4372 , Mint:MINT-1224283 , ModBase:P28632 , PR:PRO_000022919 , Protein Model Portal:P28632 , RefSeq:NP_418789 , SMR:P28632 , String:511145.b4372 , UniProt:P28632

Relationship Links: InterPro:IN-FAMILY:IPR004615 , InterPro:IN-FAMILY:IPR018382 , PDB:Structure:1EM8 , PDB:Structure:3GLI , PDB:Structure:3SXU , Pfam:IN-FAMILY:PF03603 , ProDom:IN-FAMILY:PD032475

Citations: [Xiao93b, Carter93b]

Essentiality data for holD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

References

Anderson07: Anderson SG, Williams CR, O'donnell M, Bloom LB (2007). "A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp." J Biol Chem 282(10);7035-45. PMID: 17210572

Ason00: Ason B, Bertram JG, Hingorani MM, Beechem JM, O'Donnell M, Goodman MF, Bloom LB (2000). "A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the gamma complex clamp loader." J Biol Chem 275(4);3006-15. PMID: 10644772

Ason03: Ason B, Handayani R, Williams CR, Bertram JG, Hingorani MM, O'Donnell M, Goodman MF, Bloom LB (2003). "Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp." J Biol Chem 278(12);10033-40. PMID: 12519754

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bertram00: Bertram JG, Bloom LB, Hingorani MM, Beechem JM, O'Donnell M, Goodman MF (2000). "Molecular mechanism and energetics of clamp assembly in Escherichia coli. The role of ATP hydrolysis when gamma complex loads beta on DNA." J Biol Chem 275(37);28413-20. PMID: 10874049

Bertram98: Bertram JG, Bloom LB, Turner J, O'Donnell M, Beechem JM, Goodman MF (1998). "Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Escherichia coli DNA polymerase III onto DNA." J Biol Chem 273(38);24564-74. PMID: 9733751

Blinkova93: Blinkova A, Hervas C, Stukenberg PT, Onrust R, O'Donnell ME, Walker JR (1993). "The Escherichia coli DNA polymerase III holoenzyme contains both products of the dnaX gene, tau and gamma, but only tau is essential." J Bacteriol 175(18);6018-27. PMID: 8376347

Blinkowa90: Blinkowa AL, Walker JR (1990). "Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III gamma subunit from within the tau subunit reading frame." Nucleic Acids Res 18(7);1725-9. PMID: 2186364

Bloom96: Bloom LB, Turner J, Kelman Z, Beechem JM, O'Donnell M, Goodman MF (1996). "Dynamics of loading the beta sliding clamp of DNA polymerase III onto DNA." J Biol Chem 271(48);30699-708. PMID: 8940047

Bridges90: Bridges BA, Bates H (1990). "Mutagenic DNA repair in Escherichia coli. XVIII. Involvement of DNA polymerase III alpha-subunit (DnaE protein) in mutagenesis after exposure to UV light." Mutagenesis 5(1);35-8. PMID: 2184309

Bullard02: Bullard JM, Pritchard AE, Song MS, Glover BP, Wieczorek A, Chen J, Janjic N, McHenry CS (2002). "A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme delta domain III binds delta' and assembles into the DnaX complex." J Biol Chem 277(15);13246-56. PMID: 11809766

Bunting03: Bunting KA, Roe SM, Pearl LH (2003). "Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp." EMBO J 22(21);5883-92. PMID: 14592985

Burgers81: Burgers PM, Kornberg A, Sakakibara Y (1981). "The dnaN gene codes for the beta subunit of DNA polymerase III holoenzyme of escherichia coli." Proc Natl Acad Sci U S A 78(9);5391-5. PMID: 6458041

Burgers82: Burgers PM, Kornberg A (1982). "ATP activation of DNA polymerase III holoenzyme from Escherichia coli. II. Initiation complex: stoichiometry and reactivity." J Biol Chem 257(19);11474-8. PMID: 6749841

Burgers83: Burgers PM, Kornberg A (1983). "The cycling of Escherichia coli DNA polymerase III holoenzyme in replication." J Biol Chem 258(12);7669-75. PMID: 6345527

Burnouf04: Burnouf DY, Olieric V, Wagner J, Fujii S, Reinbolt J, Fuchs RP, Dumas P (2004). "Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competition between replicative and translesion DNA polymerases." J Mol Biol 335(5);1187-97. PMID: 14729336

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Carter93: Carter JR, Franden MA, Aebersold R, McHenry CS (1993). "Identification, isolation, and characterization of the structural gene encoding the delta' subunit of Escherichia coli DNA polymerase III holoenzyme." J Bacteriol 175(12);3812-22. PMID: 8509334

Carter93a: Carter JR, Franden MA, Lippincott JA, McHenry CS (1993). "Identification, molecular cloning and characterization of the gene encoding the chi subunit of DNA polymerase III holoenzyme of Escherichia coli." Mol Gen Genet 241(3-4);399-408. PMID: 8246893

Carter93b: Carter JR, Franden MA, Aebersold R, McHenry CS (1993). "Identification, isolation, and overexpression of the gene encoding the psi subunit of DNA polymerase III holoenzyme." J Bacteriol 175(17);5604-10. PMID: 8366044

Chen93c: Chen KS, Saxena P, Walker JR (1993). "Expression of the Escherichia coli dnaX gene." J Bacteriol 175(20);6663-70. PMID: 7691799

Ciesla90: Ciesla Z, Jonczyk P, Fijalkowska I (1990). "Effect of enhanced synthesis of the epsilon subunit of DNA polymerase III on spontaneous and UV-induced mutagenesis of the Escherichia coli glyU gene." Mol Gen Genet 221(2);251-5. PMID: 2196432

CohenFix94: Cohen-Fix O, Livneh Z (1994). "In vitro UV mutagenesis associated with nucleotide excision-repair gaps in Escherichia coli." J Biol Chem 269(7);4953-8. PMID: 8106470

Conte12: Conte E, Vincelli G, Schaaper RM, Bressanin D, Stefan A, Dal Piaz F, Hochkoeppler A (2012). "Stabilization of the Escherichia coli DNA polymerase III ε subunit by the θ subunit favors in vivo assembly of the Pol III catalytic core." Arch Biochem Biophys 523(2);135-43. PMID: 22546509

Cooper93: Cooper DL, Lahue RS, Modrich P (1993). "Methyl-directed mismatch repair is bidirectional." J Biol Chem 268(16);11823-9. PMID: 8389365

Cull95: Cull MG, McHenry CS (1995). "Purification of Escherichia coli DNA polymerase III holoenzyme." Methods Enzymol 262;22-35. PMID: 8594350

Dallmann00: Dallmann HG, Kim S, Pritchard AE, Marians KJ, McHenry CS (2000). "Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks." J Biol Chem 275(20);15512-9. PMID: 10748120

Dallmann95: Dallmann HG, McHenry CS (1995). "DnaX complex of Escherichia coli DNA polymerase III holoenzyme. Physical characterization of the DnaX subunits and complexes." J Biol Chem 270(49);29563-9. PMID: 7493999

Dallmann95a: Dallmann HG, Thimmig RL, McHenry CS (1995). "DnaX complex of Escherichia coli DNA polymerase III holoenzyme. Central role of tau in initiation complex assembly and in determining the functional asymmetry of holoenzyme." J Biol Chem 270(49);29555-62. PMID: 7493998

DeRose03: DeRose EF, Darden T, Harvey S, Gabel S, Perrino FW, Schaaper RM, London RE (2003). "Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy." Biochemistry 42(13);3635-44. PMID: 12667053

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dietrich13: Dietrich M, Pedro L, Garcia J, Pons M, Huttener M, Paytubi S, Madrid C, Juarez A (2013). "Evidence for moonlighting functions of the θ subunit of Escherichia coli DNA polymerase III." J Bacteriol. PMID: 24375106

DiFrancesco84: DiFrancesco R, Bhatnagar SK, Brown A, Bessman MJ (1984). "The interaction of DNA polymerase III and the product of the Escherichia coli mutator gene, mutD." J Biol Chem 259(9);5567-73. PMID: 6325441

Dong93c: Dong Z, Onrust R, Skangalis M, O'Donnell M (1993). "DNA polymerase III accessory proteins. I. holA and holB encoding delta and delta'." J Biol Chem 268(16);11758-65. PMID: 8505303

Echols83: Echols H, Lu C, Burgers PM (1983). "Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme." Proc Natl Acad Sci U S A 80(8);2189-92. PMID: 6340117

Flower90: Flower AM, McHenry CS (1990). "The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting." Proc Natl Acad Sci U S A 87(10);3713-7. PMID: 2187190

Fradkin92: Fradkin LG, Kornberg A (1992). "Prereplicative complexes of components of DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 267(15);10318-22. PMID: 1587819

Gao01a: Gao D, McHenry CS (2001). "tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain." J Biol Chem 276(6);4433-40. PMID: 11078743

Gao01b: Gao D, McHenry CS (2001). "tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of tau, binds the replication fork, helicase, DnaB." J Biol Chem 276(6);4441-6. PMID: 11078744

Gao01c: Gao D, McHenry CS (2001). "Tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain III, shared by gamma and tau, binds delta delta ' and chi psi." J Biol Chem 276(6);4447-53. PMID: 11078742

Glover00: Glover BP, McHenry CS (2000). "The DnaX-binding subunits delta' and psi are bound to gamma and not tau in the DNA polymerase III holoenzyme." J Biol Chem 275(5);3017-20. PMID: 10652279

Glover01: Glover BP, Pritchard AE, McHenry CS (2001). "tau binds and organizes Escherichia coli replication proteins through distinct domains: domain III, shared by gamma and tau, oligomerizes DnaX." J Biol Chem 276(38);35842-6. PMID: 11463787

Glover98: Glover BP, McHenry CS (1998). "The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template." J Biol Chem 273(36);23476-84. PMID: 9722585

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Goedken04: Goedken ER, Levitus M, Johnson A, Bustamante C, O'Donnell M, Kuriyan J (2004). "Fluorescence measurements on the E.coli DNA polymerase clamp loader: implications for conformational changes during ATP and clamp binding." J Mol Biol 336(5);1047-59. PMID: 15037068

Griep88: Griep MA, McHenry CS (1988). "The dimer of the beta subunit of Escherichia coli DNA polymerase III holoenzyme is dissociated into monomers upon binding magnesium(II)." Biochemistry 27(14);5210-5. PMID: 3048397

Guenther97: Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J (1997). "Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III." Cell 91(3);335-45. PMID: 9363942

Gulbis04: Gulbis JM, Kazmirski SL, Finkelstein J, Kelman Z, O'Donnell M, Kuriyan J (2004). "Crystal structure of the chi:psi sub-assembly of the Escherichia coli DNA polymerase clamp-loader complex." Eur J Biochem 271(2);439-49. PMID: 14717711

Gupta04: Gupta R, Hamdan SM, Dixon NE, Sheil MM, Beck JL (2004). "Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase III." Protein Sci 13(11);2878-87. PMID: 15459336

Hagensee89: Hagensee ME, Moses RE (1989). "Multiple pathways for repair of hydrogen peroxide-induced DNA damage in Escherichia coli." J Bacteriol 171(2);991-5. PMID: 2644241

Hamdan02: Hamdan S, Bulloch EM, Thompson PR, Beck JL, Yang JY, Crowther JA, Lilley PE, Carr PD, Ollis DL, Brown SE, Dixon NE (2002). "Hydrolysis of the 5'-p-nitrophenyl ester of TMP by the proofreading exonuclease (epsilon) subunit of Escherichia coli DNA polymerase III." Biochemistry 41(16);5266-75. PMID: 11955076

Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523

Henson79: Henson JM, Chu H, Irwin CA, Walker JR (1979). "Isolation and characterization of dnaX and dnaY temperature-sensitive mutants of Escherichia coli." Genetics 92(4);1041-59. PMID: 391641

Hingorani98: Hingorani MM, O'Donnell M (1998). "ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme." J Biol Chem 273(38);24550-63. PMID: 9733750

Hingorani99: Hingorani MM, Bloom LB, Goodman MF, O'Donnell M (1999). "Division of labor--sequential ATP hydrolysis drives assembly of a DNA polymerase sliding clamp around DNA." EMBO J 18(18);5131-44. PMID: 10487764

Hurwitz74: Hurwitz J, Wickner S (1974). "Involvement of two protein factors and ATP in in vitro DNA synthesis catalyzed by DNA polymerase 3 of Escherichia coli." Proc Natl Acad Sci U S A 71(1);6-10. PMID: 4589895

Indiani03: Indiani C, O'Donnell M (2003). "Mechanism of the delta wrench in opening the beta sliding clamp." J Biol Chem 278(41);40272-81. PMID: 12851392

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jergic13: Jergic S, Horan NP, Elshenawy MM, Mason CE, Urathamakul T, Ozawa K, Robinson A, Goudsmits JM, Wang Y, Pan X, Beck JL, van Oijen AM, Huber T, Hamdan SM, Dixon NE (2013). "A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode." EMBO J 32(9);1322-33. PMID: 23435564

Jeruzalmi01: Jeruzalmi D, O'Donnell M, Kuriyan J (2001). "Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III." Cell 106(4);429-41. PMID: 11525729

Jeruzalmi01a: Jeruzalmi D, Yurieva O, Zhao Y, Young M, Stewart J, Hingorani M, O'Donnell M, Kuriyan J (2001). "Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III." Cell 106(4);417-28. PMID: 11525728

Johanson80: Johanson KO, McHenry CS (1980). "Purification and characterization of the beta subunit of the DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 255(22);10984-90. PMID: 6776124

Jonczyk98: Jonczyk P, Nowicka A, Fijalkowska IJ, Schaaper RM, Ciesla Z (1998). "In vivo protein interactions within the Escherichia coli DNA polymerase III core." J Bacteriol 180(6);1563-6. PMID: 9515927

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaasch89: Kaasch M, Kaasch J, Quinones A (1989). "Expression of the dnaN and dnaQ genes of Escherichia coli is inducible by mitomycin C." Mol Gen Genet 219(1-2);187-92. PMID: 2515428

Kazmirski04: Kazmirski SL, Podobnik M, Weitze TF, O'Donnell M, Kuriyan J (2004). "Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex." Proc Natl Acad Sci U S A 101(48);16750-5. PMID: 15556993

Kelman98: Kelman Z, Yuzhakov A, Andjelkovic J, O'Donnell M (1998). "Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly." EMBO J 17(8);2436-49. PMID: 9545254

Keniry00: Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE (2000). "NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli." Protein Sci 9(4);721-33. PMID: 10794414

Keniry06: Keniry MA, Park AY, Owen EA, Hamdan SM, Pintacuda G, Otting G, Dixon NE (2006). "Structure of the theta subunit of Escherichia coli DNA polymerase III in complex with the epsilon subunit." J Bacteriol 188(12);4464-73. PMID: 16740953

Keyamura11: Keyamura K, Katayama T (2011). "DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA." J Biol Chem 286(33);29336-46. PMID: 21708944

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Kim95c: Kim S, Marians KJ (1995). "DNA and RNA-DNA annealing activity associated with the tau subunit of the Escherichia coli DNA polymerase III holoenzyme." Nucleic Acids Res 23(8);1374-9. PMID: 7538662

Kim96d: Kim DR, McHenry CS (1996). "Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions. Mapping the tau binding domain of the DNA polymerase III alpha subunit." J Biol Chem 271(34);20690-8. PMID: 8702819

Kim96e: Kim DR, McHenry CS (1996). "Identification of the beta-binding domain of the alpha subunit of Escherichia coli polymerase III holoenzyme." J Biol Chem 271(34);20699-704. PMID: 8702820

Kim96f: Kim DR, McHenry CS (1996). "In vivo assembly of overproduced DNA polymerase III. Overproduction, purification, and characterization of the alpha, alpha-epsilon, and alpha-epsilon-theta subunits." J Biol Chem 271(34);20681-9. PMID: 8702818

Kim96g: Kim S, Dallmann HG, McHenry CS, Marians KJ (1996). "tau couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork." J Biol Chem 271(35);21406-12. PMID: 8702922

Kim96h: Kim S, Dallmann HG, McHenry CS, Marians KJ (1996). "Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement." Cell 84(4);643-50. PMID: 8598050

Kim96i: Kim S, Dallmann HG, McHenry CS, Marians KJ (1996). "Tau protects beta in the leading-strand polymerase complex at the replication fork." J Biol Chem 271(8);4315-8. PMID: 8626779

Kirby06: Kirby TW, Harvey S, DeRose EF, Chalov S, Chikova AK, Perrino FW, Schaaper RM, London RE, Pedersen LC (2006). "Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex." J Biol Chem 281(50):38466-71. PMID: 16973612

Kong92: Kong XP, Onrust R, O'Donnell M, Kuriyan J (1992). "Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp." Cell 69(3);425-37. PMID: 1349852

Kornberg72: Kornberg T, Gefter ML (1972). "Deoxyribonucleic acid synthesis in cell-free extracts. IV. Purification and catalytic properties of deoxyribonucleic acid polymerase III." J Biol Chem 247(17);5369-75. PMID: 4560196

Kozlov10: Kozlov AG, Jezewska MJ, Bujalowski W, Lohman TM (2010). "Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase." Biochemistry 49(17);3555-66. PMID: 20329707

Kurz04: Kurz M, Dalrymple B, Wijffels G, Kongsuwan K (2004). "Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein." J Bacteriol 186(11);3508-15. PMID: 15150238

LaDuca83: LaDuca RJ, Fay PJ, Chuang C, McHenry CS, Bambara RA (1983). "Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III." Biochemistry 22(22);5177-88. PMID: 6360204

LaDuca86: LaDuca RJ, Crute JJ, McHenry CS, Bambara RA (1986). "The beta subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits." J Biol Chem 261(16);7550-7. PMID: 3519609

Lamers06: Lamers MH, Georgescu RE, Lee SG, O'Donnell M, Kuriyan J (2006). "Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III." Cell 126(5);881-92. PMID: 16959568

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lee87: Lee SH, Walker JR (1987). "Escherichia coli DnaX product, the tau subunit of DNA polymerase III, is a multifunctional protein with single-stranded DNA-dependent ATPase activity." Proc Natl Acad Sci U S A 84(9);2713-7. PMID: 3033660

Leu00: Leu FP, Hingorani MM, Turner J, O'Donnell M (2000). "The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli." J Biol Chem 275(44);34609-18. PMID: 10924523

Leu01: Leu FP, O'Donnell M (2001). "Interplay of clamp loader subunits in opening the beta sliding clamp of Escherichia coli DNA polymerase III holoenzyme." J Biol Chem 276(50);47185-94. PMID: 11572866

Li08b: Li F, Liu Q, Chen YY, Yu ZN, Zhang ZP, Zhou YF, Deng JY, Bi LJ, Zhang XE (2008). "Escherichia coli mismatch repair protein MutL interacts with the clamp loader subunits of DNA polymerase III." Mutat Res 637(1-2);101-10. PMID: 17765269

Li99d: Li D, Allen DL, Harvey S, Perrino FW, Schaaper RM, London RE (1999). "A preliminary CD and NMR study of the Escherichia coli DNA polymerase III theta subunit." Proteins 36(1);111-6. PMID: 10373010

Livingston75: Livingston DM, Hinkle DC, Richardson CC (1975). "Deoxyribonucleic acid polymerase III of Escherichia coli. Purification and properties." J Biol Chem 250(2);461-9. PMID: 1089643

Livingston75a: Livingston DM, Richardson CC (1975). "Deoxyribonucleic acid polymerase III of Escherichia coli. Characterization of associated exonuclease activities." J Biol Chem 250(2);470-8. PMID: 163228

Livneh86: Livneh Z (1986). "Mechanism of replication of ultraviolet-irradiated single-stranded DNA by DNA polymerase III holoenzyme of Escherichia coli. Implications for SOS mutagenesis." J Biol Chem 261(20);9526-33. PMID: 2941423

Lopez03: Lopez de Saro FJ, Georgescu RE, Goodman MF, O'Donnell M (2003). "Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair." EMBO J 22(23);6408-18. PMID: 14633999

Lopez03a: Lopez de Saro FJ, Georgescu RE, O'Donnell M (2003). "A peptide switch regulates DNA polymerase processivity." Proc Natl Acad Sci U S A 100(25);14689-94. PMID: 14630952

Macian94: Macian F, Perez-Roger I, Armengod ME (1994). "An improved vector system for constructing transcriptional lacZ fusions: analysis of regulation of the dnaA, dnaN, recF and gyrB genes of Escherichia coli." Gene 1994;145(1);17-24. PMID: 8045420

Magdalena04: Magdalena Coman M, Jin M, Ceapa R, Finkelstein J, O'Donnell M, Chait BT, Hingorani MM (2004). "Dual functions, clamp opening and primer-template recognition, define a key clamp loader subunit." J Mol Biol 342(5);1457-69. PMID: 15364574

Maki85: Maki H, Kornberg A (1985). "The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the alpha subunit, devoid of nuclease activities." J Biol Chem 260(24);12987-92. PMID: 2997151

Maki87: Maki H, Kornberg A (1987). "Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunits." Proc Natl Acad Sci U S A 84(13);4389-92. PMID: 3037519

Maki88: Maki S, Kornberg A (1988). "DNA polymerase III holoenzyme of Escherichia coli. III. Distinctive processive polymerases reconstituted from purified subunits." J Biol Chem 263(14);6561-9. PMID: 3283127

Maki88a: Maki S, Kornberg A (1988). "DNA polymerase III holoenzyme of Escherichia coli. II. A novel complex including the gamma subunit essential for processive synthesis." J Biol Chem 263(14);6555-60. PMID: 3283126

Maki88b: Maki H, Maki S, Kornberg A (1988). "DNA Polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites." J Biol Chem 263(14);6570-8. PMID: 3283128

Maki90: Maki H, Akiyama M, Horiuchi T, Sekiguchi M (1990). "Molecular mechanisms of replicational fidelity in Escherichia coli." Basic Life Sci 52;299-308. PMID: 2158294

Marceau11: Marceau AH, Bahng S, Massoni SC, George NP, Sandler SJ, Marians KJ, Keck JL (2011). "Structure of the SSB-DNA polymerase III interface and its role in DNA replication." EMBO J 30(20);4236-47. PMID: 21857649

McHenry79: McHenry CS, Crow W (1979). "DNA polymerase III of Escherichia coli. Purification and identification of subunits." J Biol Chem 254(5);1748-53. PMID: 368075

Morag99: Morag AS, Saveson CJ, Lovett ST (1999). "Expansion of DNA repeats in Escherichia coli: effects of recombination and replication functions." J Mol Biol 289(1);21-7. PMID: 10339402

Motamedi99: Motamedi MR, Szigety SK, Rosenberg SM (1999). "Double-strand-break repair recombination in Escherichia coli: physical evidence for a DNA replication mechanism in vivo." Genes Dev 13(21);2889-903. PMID: 10557215

Mueller05: Mueller GA, Kirby TW, DeRose EF, Li D, Schaaper RM, London RE (2005). "Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit." J Bacteriol 187(20);7081-9. PMID: 16199579

Naktinis95: Naktinis V, Onrust R, Fang L, O'Donnell M (1995). "Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp." J Biol Chem 270(22);13358-65. PMID: 7768937

Nusslein76: Nusslein V, Henke S, Johnston LH (1976). "Replication of E. coli duplex DNA in vitro. The separation of the DNA containing fractions of a lysate from the soluble enzymes and their complementation properties." Mol Gen Genet 145(2);183-90. PMID: 778584

Oakley03: Oakley AJ, Prosselkov P, Wijffels G, Beck JL, Wilce MC, Dixon NE (2003). "Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III." Acta Crystallogr D Biol Crystallogr 59(Pt 7);1192-9. PMID: 12832762

ODonnell85: O'Donnell ME, Kornberg A (1985). "Dynamics of DNA polymerase III holoenzyme of Escherichia coli in replication of a multiprimed template." J Biol Chem 260(23);12875-83. PMID: 2413035

ODonnell87: O'Donnell ME (1987). "Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli." J Biol Chem 262(34);16558-65. PMID: 3316222

Oishi06: Oishi Y, Yunomura S, Kawahashi Y, Doi N, Takashima H, Baba T, Mori H, Yanagawa H (2006). "Escherichia coli proteome chips for detecting protein-protein interactions." Proteomics 6(24);6433-6. PMID: 17109382

Olson95: Olson MW, Dallmann HG, McHenry CS (1995). "DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant range." J Biol Chem 270(49);29570-7. PMID: 7494000

Onogi02: Onogi T, Ohsumi K, Katayama T, Hiraga S (2002). "Replication-dependent recruitment of the beta-subunit of DNA polymerase III from cytosolic spaces to replication forks in Escherichia coli." J Bacteriol 184(3);867-70. PMID: 11790763

Onrust95: Onrust R, Finkelstein J, Turner J, Naktinis V, O'Donnell M (1995). "Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader." J Biol Chem 270(22);13366-77. PMID: 7768938

Onrust95a: Onrust R, Finkelstein J, Naktinis V, Turner J, Fang L, O'Donnell M (1995). "Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader." J Biol Chem 270(22);13348-57. PMID: 7768936

Ozawa08: Ozawa K, Jergic S, Park AY, Dixon NE, Otting G (2008). "The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker." Nucleic Acids Res 36(15);5074-82. PMID: 18663010

Ozawa13: Ozawa K, Horan NP, Robinson A, Yagi H, Hill FR, Jergic S, Xu ZQ, Loscha KV, Li N, Tehei M, Oakley AJ, Otting G, Huber T, Dixon NE (2013). "Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain." Nucleic Acids Res 41(10);5354-67. PMID: 23580545

Pages05: Pages V, Janel-Bintz R, Fuchs RP (2005). "Pol III proofreading activity prevents lesion bypass as evidenced by its molecular signature within E.coli cells." J Mol Biol 352(3);501-9. PMID: 16111701

Parks09: Parks AR, Li Z, Shi Q, Owens RM, Jin MM, Peters JE (2009). "Transposition into replicating DNA occurs through interaction with the processivity factor." Cell 138(4);685-95. PMID: 19703395

PazElizur96: Paz-Elizur T, Skaliter R, Blumenstein S, Livneh Z (1996). "Beta*, a UV-inducible smaller form of the beta subunit sliding clamp of DNA polymerase III of Escherichia coli. I. Gene expression and regulation." J Biol Chem 271(5);2482-90. PMID: 8576211

PerezRoger91: Perez-Roger I, Garcia-Sogo M, Navarro-Avino JP, Lopez-Acedo C, Macian F, Armengod ME (1991). "Positive and negative regulatory elements in the dnaA-dnaN-recF operon of Escherichia coli." Biochimie 73(2-3);329-34. PMID: 1883890

Pintacuda06: Pintacuda G, Park AY, Keniry MA, Dixon NE, Otting G (2006). "Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes." J Am Chem Soc 128(11);3696-702. PMID: 16536542

Pritchard00: Pritchard AE, Dallmann HG, Glover BP, McHenry CS (2000). "A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'." EMBO J 19(23);6536-45. PMID: 11101526

Quillardet03: Quillardet P, Rouffaud MA, Bouige P (2003). "DNA array analysis of gene expression in response to UV irradiation in Escherichia coli." Res Microbiol 154(8);559-72. PMID: 14527657

Quinones88: Quinones A, Piechocki R, Messer W (1988). "Expression of the Escherichia coli dnaQ (mutD) gene is inducible." Mol Gen Genet 211(1);106-12. PMID: 2830459

Quinones89: Quinones A, Kaasch J, Kaasch M, Messer W (1989). "Induction of dnaN and dnaQ gene expression in Escherichia coli by alkylation damage to DNA." EMBO J 8(2);587-93. PMID: 2656258

Quinones90: Quinones A (1990). "Regulation of the dnaQ gene of Escherichia coli in mutants expressing the SOS regulon constitutively." J Basic Microbiol 30(5);353-62. PMID: 2242163

Rajagopala09: Rajagopala SV, Hughes KT, Uetz P (2009). "Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins." Proteomics 9(23);5296-302. PMID: 19834901

Rajagopala12: Rajagopala SV, Sikorski P, Caufield JH, Tovchigrechko A, Uetz P (2012). "Studying protein complexes by the yeast two-hybrid system." Methods 58(4);392-9. PMID: 22841565

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reems94: Reems JA, McHenry CS (1994). "Escherichia coli DNA polymerase III holoenzyme footprints three helical turns of its primer." J Biol Chem 269(52);33091-6. PMID: 7806536

Reems95: Reems JA, Wood S, McHenry CS (1995). "Escherichia coli DNA polymerase III holoenzyme subunits alpha, beta, and gamma directly contact the primer-template." J Biol Chem 270(10);5606-13. PMID: 7890680

ReyesLamothe10: Reyes-Lamothe R, Sherratt DJ, Leake MC (2010). "Stoichiometry and architecture of active DNA replication machinery in Escherichia coli." Science 328(5977);498-501. PMID: 20413500

Scheuermann83: Scheuermann R, Tam S, Burgers PM, Lu C, Echols H (1983). "Identification of the epsilon-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: a fidelity subunit for DNA replication." Proc Natl Acad Sci U S A 80(23);7085-9. PMID: 6359162

Scheuermann84: Scheuermann RH, Echols H (1984). "A separate editing exonuclease for DNA replication: the epsilon subunit of Escherichia coli DNA polymerase III holoenzyme." Proc Natl Acad Sci U S A 81(24);7747-51. PMID: 6393125

Sharif90: Sharif F, Bridges BA (1990). "Mutagenic DNA repair in Escherichia coli. XVII. Effect of temperature-sensitive DnaE proteins on the induction of streptomycin-resistant mutations by UV light." Mutagenesis 5(1);31-4. PMID: 2184308

Shavitt89: Shavitt O, Livneh Z (1989). "The beta subunit modulates bypass and termination at UV lesions during in vitro replication with DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 264(19);11275-81. PMID: 2661556

Shwartz87: Shwartz H, Livneh Z (1987). "Dynamics of termination during in vitro replication of ultraviolet-irradiated DNA with DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 262(22);10518-23. PMID: 2956258

Shwartz88: Shwartz H, Shavitt O, Livneh Z (1988). "The role of exonucleolytic processing and polymerase-DNA association in bypass of lesions during replication in vitro. Significance for SOS-targeted mutagenesis." J Biol Chem 263(34);18277-85. PMID: 3056941

Simonetta09: Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J (2009). "The mechanism of ATP-dependent primer-template recognition by a clamp loader complex." Cell 137(4);659-71. PMID: 19450514

Skaliter96: Skaliter R, Bergstein M, Livneh Z (1996). "Beta*, a UV-inducible shorter form of the beta subunit of DNA polymerase III of Escherichia coli. II. Overproduction, purification, and activity as a polymerase processivity clamp." J Biol Chem 271(5);2491-6. PMID: 8576212

Skaliter96a: Skaliter R, Paz-Elizur T, Livneh Z (1996). "A smaller form of the sliding clamp subunit of DNA polymerase III is induced by UV irradiation in Escherichia coli." J Biol Chem 271(5);2478-81. PMID: 8576210

Slater94: Slater SC, Lifsics MR, O'Donnell M, Maurer R (1994). "holE, the gene coding for the theta subunit of DNA polymerase III of Escherichia coli: characterization of a holE mutant and comparison with a dnaQ (epsilon-subunit) mutant." J Bacteriol 176(3);815-21. PMID: 8300534

Snyder04: Snyder AK, Williams CR, Johnson A, O'Donnell M, Bloom LB (2004). "Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the beta and DNA binding activities of the gamma complex." J Biol Chem 279(6);4386-93. PMID: 14610068

Song01a: Song MS, McHenry CS (2001). "Carboxyl-terminal domain III of the delta' subunit of DNA polymerase III holoenzyme binds DnaX and supports cooperative DnaX complex assembly." J Biol Chem 276(52);48709-15. PMID: 11606586

Song01b: Song MS, Dallmann HG, McHenry CS (2001). "Carboxyl-terminal domain III of the delta' subunit of the DNA polymerase III holoenzyme binds delta." J Biol Chem 276(44);40668-79. PMID: 11518714

Studwell90: Studwell PS, O'Donnell M (1990). "Processive replication is contingent on the exonuclease subunit of DNA polymerase III holoenzyme." J Biol Chem 265(2);1171-8. PMID: 2153103

StudwellVaughan91: Studwell-Vaughan PS, O'Donnell M (1991). "Constitution of the twin polymerase of DNA polymerase III holoenzyme." J Biol Chem 266(29);19833-41. PMID: 1918087

StudwellVaughan93: Studwell-Vaughan PS, O'Donnell M (1993). "DNA polymerase III accessory proteins. V. Theta encoded by holE." J Biol Chem 268(16);11785-91. PMID: 8505306

Stukenberg91: Stukenberg PT, Studwell-Vaughan PS, O'Donnell M (1991). "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme." J Biol Chem 266(17);11328-34. PMID: 2040637

Sutton05: Sutton MD, Duzen JM, Maul RW (2005). "Mutant forms of the Escherichia colibeta sliding clamp that distinguish between its roles in replication and DNA polymerase V-dependent translesion DNA synthesis." Mol Microbiol 55(6);1751-66. PMID: 15752198

Suzuki98b: Suzuki E, Kondo T, Makise M, Mima S, Sakamoto K, Tsuchiya T, Mizushima T (1998). "Alteration in levels of unsaturated fatty acids in mutants of Escherichia coli defective in DNA replication." Biol Pharm Bull 21(7);657-61. PMID: 9703244

Tadmor94: Tadmor Y, Bergstein M, Skaliter R, Shwartz H, Livneh Z (1994). "Beta subunit of DNA polymerase III holoenzyme is induced upon ultraviolet irradiation or nalidixic acid treatment of Escherichia coli." Mutat Res 308(1);53-64. PMID: 7516486

TaftBenz04: Taft-Benz SA, Schaaper RM (2004). "The theta subunit of Escherichia coli DNA polymerase III: a role in stabilizing the epsilon proofreading subunit." J Bacteriol 186(9);2774-80. PMID: 15090519

Tomer96: Tomer G, Cohen-Fix O, O'Donnell M, Goodman M, Livneh Z (1996). "Reconstitution of repair-gap UV mutagenesis with purified proteins from Escherichia coli: a role for DNA polymerases III and II." Proc Natl Acad Sci U S A 93(4);1376-80. PMID: 8643639

Toste13: Toste Rego A, Holding AN, Kent H, Lamers MH (2013). "Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair." EMBO J 32(9);1334-43. PMID: 23549287

Tsuchihashi89: Tsuchihashi Z, Kornberg A (1989). "ATP interactions of the tau and gamma subunits of DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 264(30);17790-5. PMID: 2681183

Tsuchihashi90: Tsuchihashi Z, Kornberg A (1990). "Translational frameshifting generates the gamma subunit of DNA polymerase III holoenzyme." Proc Natl Acad Sci U S A 87(7);2516-20. PMID: 2181440

Turner99: Turner J, Hingorani MM, Kelman Z, O'Donnell M (1999). "The internal workings of a DNA polymerase clamp-loading machine." EMBO J 18(3);771-83. PMID: 9927437

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Van01a: Van Dyk TK, DeRose EJ, Gonye GE (2001). "LuxArray, a high-density, genomewide transcription analysis of Escherichia coli using bioluminescent reporter strains." J Bacteriol 183(19);5496-505. PMID: 11544210

Villarroya98: Villarroya M, Perez-Roger I, Macian F, Armengod ME (1998). "Stationary phase induction of dnaN and recF, two genes of Escherichia coli involved in DNA replication and repair." EMBO J 17(6);1829-37. PMID: 9501104

Walker00: Walker JR, Hervas C, Ross JD, Blinkova A, Walbridge MJ, Pumarega EJ, Park MO, Neely HR (2000). "Escherichia coli DNA polymerase III tau- and gamma-subunit conserved residues required for activity in vivo and in vitro." J Bacteriol 182(21);6106-13. PMID: 11029431

Welch82: Welch MM, McHenry CS (1982). "Cloning and identification of the product of the dnaE gene of Escherichia coli." J Bacteriol 152(1);351-6. PMID: 6288664

Wieczorek06: Wieczorek A, McHenry CS (2006). "The NH2-terminal php domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit." J Biol Chem 281(18):12561-7. PMID: 16517598

Wijffels04: Wijffels G, Dalrymple BP, Prosselkov P, Kongsuwan K, Epa VC, Lilley PE, Jergic S, Buchardt J, Brown SE, Alewood PF, Jennings PA, Dixon NE (2004). "Inhibition of protein interactions with the beta 2 sliding clamp of Escherichia coli DNA polymerase III by peptides from beta 2-binding proteins." Biochemistry 43(19);5661-71. PMID: 15134440

Williams04: Williams CR, Snyder AK, Kuzmic P, O'Donnell M, Bloom LB (2004). "Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: I. Two distinct activities for individual ATP sites in the gamma complex." J Biol Chem 279(6);4376-85. PMID: 14610067

Witkin92: Witkin EM, Roegner-Maniscalco V (1992). "Overproduction of DnaE protein (alpha subunit of DNA polymerase III) restores viability in a conditionally inviable Escherichia coli strain deficient in DNA polymerase I." J Bacteriol 174(12);4166-8. PMID: 1597430

Witte03: Witte G, Urbanke C, Curth U (2003). "DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery." Nucleic Acids Res 31(15);4434-40. PMID: 12888503

Woodgate87: Woodgate R, Bridges BA, Herrera G, Blanco M (1987). "Mutagenic DNA repair in Escherichia coli. XIII. Proofreading exonuclease of DNA polymerase III holoenzyme is not operational during UV mutagenesis." Mutat Res 183(1);31-7. PMID: 3025722

Wu90: Wu TH, Clarke CH, Marinus MG (1990). "Specificity of Escherichia coli mutD and mutL mutator strains." Gene 87(1);1-5. PMID: 2185133

Xiao93a: Xiao H, Dong Z, O'Donnell M (1993). "DNA polymerase III accessory proteins. IV. Characterization of chi and psi." J Biol Chem 268(16);11779-84. PMID: 8505305

Xiao93b: Xiao H, Crombie R, Dong Z, Onrust R, O'Donnell M (1993). "DNA polymerase III accessory proteins. III. holC and holD encoding chi and psi." J Biol Chem 268(16);11773-8. PMID: 8389364

Yao00: Yao N, Leu FP, Anjelkovic J, Turner J, O'Donnell M (2000). "DNA structure requirements for the Escherichia coli gamma complex clamp loader and DNA polymerase III holoenzyme." J Biol Chem 275(15);11440-50. PMID: 10753961

Yong13: Yong HT, Yamamoto N, Takeuchi R, Hsieh YJ, Conrad TM, Datsenko KA, Nakayashiki T, Wanner BL, Mori H (2013). "Development of a system for discovery of genetic interactions for essential genes in Escherichia coli K-12." Genes Genet Syst 88(4);233-40. PMID: 24463526

Yuzhakov99: Yuzhakov A, Kelman Z, O'Donnell M (1999). "Trading places on DNA--a three-point switch underlies primer handoff from primase to the replicative DNA polymerase." Cell 96(1);153-63. PMID: 9989506

Zahra07: Zahra R, Blackwood JK, Sales J, Leach DR (2007). "Proofreading and Secondary Structure Processing Determine the Orientation Dependence of CAG{middle dot}CTG Trinucleotide Repeat Instability in Escherichia coli." Genetics 176(1):27-41. PMID: 17339223

Zechner92: Zechner EL, Wu CA, Marians KJ (1992). "Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. III. A polymerase-primase interaction governs primer size." J Biol Chem 267(6);4054-63. PMID: 1531480


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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