Escherichia coli K-12 substr. MG1655 Enzyme: endonuclease III

Gene: nth Accession Numbers: EG10662 (EcoCyc), b1633, ECK1629

Synonyms: Endo III

Regulation Summary Diagram: ?

Regulation summary diagram for nth

Endonuclease III (Endo III or Nth) is a combined DNA glycosylase and apurinic/apyrimidinic (AP) lyase that cleaves the N-glycosidic bond of damaged pyrimidine residues and removes the 3' phosphate at the apyrimidinic site. Endo III catalysis generates DNA strand breaks that are 3' to the abasic site; it creates blocked 3' termini that are then processed by one of two AP endonucleases (Exonuclease III and Endonuclease IV) to generate the 3' OH ends that are required for DNA polymerase repair synthesis (see [Mol00])

Endonuclease III recognizes pyrimidine residues damaged by ring saturation, ring fragmentation or ring contraction. Examples of these types of damage include: thymine glycol, 5,6-dihydrothymine, 5,6-dihydrouracil, alloxan, uracil glycol, 5-hydroxy-6-hydrothymine, 5-hydroxy-6-hydrouracil, [Dizdaroglu93, Purmal98] 5-hydroxycytosine, 5-hydroxyuracil [Hatahet94], 5,6-dihydroxyuracil, 5,6-dihydroxycytosine [Dizdaroglu00] and others [Breimer84, DHam99, Asagoshi00].

Endo III generates single strand breaks (nicks) in UV damaged duplex DNA [Radman76, Gates77]. Endo III is a DNA glycosylase that excises thymine oxidation products [Demple80]. Endo III has 3' AP endonuclease activity; nicks generated by Endo III have low priming activity with DNA polymerase I [Warner80]. Endo III is an AP lyase; Endo III cleaves 3' to AP sites by a β-elimination mechanism with formation of a trans α,-β unsaturated aldose [Bailly87, Kim88, Mazumder91]. Endo III cleaves 5-fluorouracil and 5-formyluracil containing oligonucleotides with formation of a 5' fragment containing a 3'-deoxyribose phosphate (not an α-β unsaturated aldose) [Darwanto09].

Endo III contains a [4Fe-4S] cluster [Cunningham89]. The Fe-S cluster is not directly involved in catalysis, it may have a structural or regulatory role [Fu92]. The Fe-S cluster is redox active when bound to DNA invitro and a model for detecting DNA damage based on DNA mediated redox signalling between repair enzymes has been proposed [Boal05].

The protein is primarily α helical in structure and can be divided into two domains - a 6 helix barrel domain (residues 22-132) and a [4Fe-4S] cluster domain (residues 1-21 and 133-211) - which are separated by a deep cleft or groove [Kuo92]. An active site pocket exists within the interdomain groove and is bracketed by two DNA binding regions: a helix-hairpin-helix (HhH) domain (residues108-127) and a [4Fe-4S] cluster loop (FCL) (residues 186-194) [Thayer95].

Endo III searches for damage by diffusing along DNA and probing for damaged bases; Endo III contains a key 'wedge' residue (Leu81) believed to scan for DNA damage by inserting into the duplex and testing for strength and flexibility of base pairs. Mutation of this residue (L81A) results in faster diffusion of the enzyme along a DNA substrate in vitro [Dunn11, Nelson14]

Endonuclease III crosslinks to 2-deoxyribonolactone DNA lesions; such lesions interfere with endonuclease III excision repair of abasic lesions [Kroeger03].

Endo III is the representative member of the helix-hairpin-helix (HhH) superfamily of DNA glycosylases.

Reviews: [Cunningham94, Lukianova05, Lee14b]
Comment: [Brosh12]

Citations: [Weiss85, BricteuxGregoir89, Dodson94, Chaudhry95, Wagner96, Saito97a, DHam98, Harrison98, Jurado98, Serafini99, Zhang00, Gifford00, Piersen00, Matsumoto01, Hazra01, Tano01, Hori03, Janion03, Denver03, Miller04, Lomax05, Wiederholt05, Watanabe05, Doi06, Boal07, Suzuki08, Romano11, Sontz12, Grodick14, Kuznetsov15, DavidCordonnier01]

Gene Citations: [Gifford00]

Locations: cytosol

Map Position: [1,709,547 -> 1,710,182] (36.85 centisomes, 133°)
Length: 636 bp / 211 aa

Molecular Weight of Polypeptide: 23.562 kD (from nucleotide sequence), 27.3 kD (experimental) [Asahara89 ]

Unification Links: ASAP:ABE-0005463 , CGSC:13070 , DIP:DIP-48071N , EchoBASE:EB0656 , EcoGene:EG10662 , EcoliWiki:b1633 , Mint:MINT-1223379 , ModBase:P0AB83 , OU-Microarray:b1633 , PortEco:nth , PR:PRO_000023419 , Protein Model Portal:P0AB83 , RefSeq:NP_416150 , RegulonDB:EG10662 , SMR:P0AB83 , String:511145.b1633 , UniProt:P0AB83

Relationship Links: InterPro:IN-FAMILY:IPR000445 , InterPro:IN-FAMILY:IPR003265 , InterPro:IN-FAMILY:IPR003583 , InterPro:IN-FAMILY:IPR003651 , InterPro:IN-FAMILY:IPR004035 , InterPro:IN-FAMILY:IPR004036 , InterPro:IN-FAMILY:IPR005759 , InterPro:IN-FAMILY:IPR011257 , InterPro:IN-FAMILY:IPR023170 , PDB:Structure:2ABK , Pfam:IN-FAMILY:PF00633 , Pfam:IN-FAMILY:PF00730 , Pfam:IN-FAMILY:PF10576 , Prosite:IN-FAMILY:PS00764 , Prosite:IN-FAMILY:PS01155 , Smart:IN-FAMILY:SM00278 , Smart:IN-FAMILY:SM00478 , Smart:IN-FAMILY:SM00525

In Paralogous Gene Group: 322 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006285 - base-excision repair, AP site formation Inferred from experiment [Warner80, Kim88, Asahara89]
GO:0034644 - cellular response to UV Inferred from experiment [Radman76]
GO:0006281 - DNA repair Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0006284 - base-excision repair Inferred by computational analysis [GOA01a]
GO:0006974 - cellular response to DNA damage stimulus Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000703 - oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Inferred from experiment [Dizdaroglu93, Demple80, Warner80, Asahara89]
GO:0003906 - DNA-(apurinic or apyrimidinic site) lyase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Kim88, Mazumder91]
GO:0005515 - protein binding Inferred from experiment [Butland05]
GO:0019104 - DNA N-glycosylase activity Inferred from experiment Inferred by computational analysis [GOA06, Asahara89]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Cunningham89, Kuo92]
GO:0003677 - DNA binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11a]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell processes protection radiation
information transfer DNA related DNA repair

Essentiality data for nth knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
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]

Revised 20-May-2015 by Mackie A , Macquarie University
Last-Curated ? 21-May-2015 by Mackie A , Macquarie University

Enzymatic reaction of: DNA glycosylase (endonuclease III)

EC Number:

a damaged DNA pyrimidine <=> a DNA containing an apyrimidinic site

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Enzymatic reaction of: DNA-AP site lyase (endonuclease III)

EC Number:

a DNA containing an apurinic/apyrimidinic site <=> a 5'-phosphopolynucleotide + a 3'-terminal unsaturated sugar

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Sequence Features

Protein sequence of endonuclease III with features indicated

Feature Class Location Common Name Citations Comment
Alpha-Helix-Region 3 -> 16 αA
Alpha-Helix-Region 29 -> 39 αB
Alpha-Helix-Region 44 -> 56 αC
Alpha-Helix-Region 61 -> 67 αD1
Alpha-Helix-Region 69 -> 75 αD2
Mutagenesis-Variant 81  
alternate sequence L → A: mutant protein has faster diffusive behaviour on DNA substrate in vitro
Alpha-Helix-Region 82 -> 99 αE
Alpha-Helix-Region 107 -> 113 αF
DNA-Binding-Region 108 -> 127 HhH domain
helix-hairpin-helix domain implicated in DNA binding
Conserved-Region 108 -> 127  
UniProt: HhH.
Protein-Binding-Region 113 -> 119 β hairpin
thymine glycol binding
Alpha-Helix-Region 119 -> 129 αG
Mutagenesis-Variant 120  
[Thayer95, UniProt13]
UniProt: 100000-fold decrease in activity and slight decrease in substrate affinity.
Alpha-Helix-Region 138 -> 148 αH
Mutagenesis-Variant 138  
[Thayer95, UniProt13]
UniProt: 100-fold decrease in activity and 4-fold increase in substrate affinity.
Alpha-Helix-Region 156 -> 166 αI
Alpha-Helix-Region 175 -> 185 αJ
DNA-Binding-Region 186 -> 194 FCL domain
[4Fe-4S] cluster loop (FCL) implicated in DNA binding
Metal-Binding-Site 187  
[UniProt15, Kuo92]
UniProt: Iron-sulfur (4Fe-4S).
Mutagenesis-Variant 191  
[Thayer95, UniProt13]
UniProt: Slight decrease in activity and 130-fold increase in substrate affinity.
Metal-Binding-Site 194  
[UniProt15, Kuo92]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 197  
[UniProt15, Kuo92]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 203  
[UniProt15, Kuo92]
UniProt: Iron-sulfur (4Fe-4S).

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b1633 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10662; confirmed by SwissProt match.


Asagoshi00: Asagoshi K, Odawara H, Nakano H, Miyano T, Terato H, Ohyama Y, Seki S, Ide H (2000). "Comparison of substrate specificities of Escherichia coli endonuclease III and its mouse homologue (mNTH1) using defined oligonucleotide substrates." Biochemistry 39(37);11389-98. PMID: 10985784

Asahara89: Asahara H, Wistort PM, Bank JF, Bakerian RH, Cunningham RP (1989). "Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene." Biochemistry 28(10);4444-9. PMID: 2669955

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

Bailly87: Bailly V, Verly WG (1987). "Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst." Biochem J 242(2);565-72. PMID: 2439070

Boal05: Boal AK, Yavin E, Lukianova OA, O'Shea VL, David SS, Barton JK (2005). "DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters." Biochemistry 44(23);8397-407. PMID: 15938629

Boal07: Boal AK, Yavin E, Barton JK (2007). "DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport?." J Inorg Biochem 101(11-12);1913-21. PMID: 17599416

Breimer84: Breimer LH, Lindahl T (1984). "DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli." J Biol Chem 259(9);5543-8. PMID: 6371006

BricteuxGregoir89: Bricteux-Gregoire S, Verly WG (1989). "The use of thioglycolate to distinguish between 3' AP (apurinic/apyrimidinic) endonucleases and AP lyases." Nucleic Acids Res 17(15);6269-82. PMID: 2475855

Brosh12: Brosh RM (2012). "Finding a needle in the haystack: recognition of DNA damage by collaboration between DNA repair proteins able to perform DNA charge transport." Cell Cycle 11(6);1055-6. PMID: 22377696

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

Chaudhry95: Chaudhry MA, Weinfeld M (1995). "The action of Escherichia coli endonuclease III on multiply damaged sites in DNA." J Mol Biol 249(5);914-22. PMID: 7791217

Cunningham89: Cunningham RP, Asahara H, Bank JF, Scholes CP, Salerno JC, Surerus K, Munck E, McCracken J, Peisach J, Emptage MH (1989). "Endonuclease III is an iron-sulfur protein." Biochemistry 28(10);4450-5. PMID: 2548577

Cunningham94: Cunningham RP, Ahern H, Xing D, Thayer MM, Tainer JA (1994). "Structure and function of Escherichia coli endonuclease III." Ann N Y Acad Sci 726;215-22. PMID: 8092678

Darwanto09: Darwanto A, Farrel A, Rogstad DK, Sowers LC (2009). "Characterization of DNA glycosylase activity by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry." Anal Biochem 394(1);13-23. PMID: 19607800

DavidCordonnier01: David-Cordonnier MH, Laval J, O'Neill P (2001). "Recognition and kinetics for excision of a base lesion within clustered DNA damage by the Escherichia coli proteins Fpg and Nth." Biochemistry 40(19);5738-46. PMID: 11341839

Demple80: Demple B, Linn S (1980). "DNA N-glycosylases and UV repair." Nature 287(5779);203-8. PMID: 6253795

Denver03: Denver DR, Swenson SL, Lynch M (2003). "An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases." Mol Biol Evol 20(10);1603-11. PMID: 12832627

DHam98: D'Ham C, Ravanat JL, Cadet J (1998). "Gas chromatography-mass spectrometry with high-performance liquid chromatography prepurification for monitoring the endonuclease III-mediated excision of 5-hydroxy-5,6-dihydrothymine and 5,6-dihydrothymine from gamma-irradiated DNA." J Chromatogr B Biomed Sci Appl 710(1-2);67-74. PMID: 9686872

DHam99: D'Ham C, Romieu A, Jaquinod M, Gasparutto D, Cadet J (1999). "Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins: kinetic and mechanistic aspects." Biochemistry 38(11);3335-44. PMID: 10079077

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

Dizdaroglu00: Dizdaroglu M, Bauche C, Rodriguez H, Laval J (2000). "Novel substrates of Escherichia coli nth protein and its kinetics for excision of modified bases from DNA damaged by free radicals." Biochemistry 39(18);5586-92. PMID: 10820032

Dizdaroglu93: Dizdaroglu M, Laval J, Boiteux S (1993). "Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals." Biochemistry 32(45);12105-11. PMID: 8218289

Dodson94: Dodson ML, Michaels ML, Lloyd RS (1994). "Unified catalytic mechanism for DNA glycosylases." J Biol Chem 269(52);32709-12. PMID: 7806489

Doi06: Doi Y, Katafuchi A, Fujiwara Y, Hitomi K, Tainer JA, Ide H, Iwai S (2006). "Synthesis and characterization of oligonucleotides containing 2'-fluorinated thymidine glycol as inhibitors of the endonuclease III reaction." Nucleic Acids Res 34(5);1540-51. PMID: 16547199

Dunn11: Dunn AR, Kad NM, Nelson SR, Warshaw DM, Wallace SS (2011). "Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA." Nucleic Acids Res 39(17);7487-98. PMID: 21666255

Fu92: Fu W, O'Handley S, Cunningham RP, Johnson MK (1992). "The role of the iron-sulfur cluster in Escherichia coli endonuclease III. A resonance Raman study." J Biol Chem 267(23);16135-7. PMID: 1644800

Gates77: Gates FT, Linn S (1977). "Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays." J Biol Chem 252(9);2802-7. PMID: 16001

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gifford00: Gifford CM, Wallace SS (2000). "The genes encoding endonuclease VIII and endonuclease III in Escherichia coli are transcribed as the terminal genes in operons." Nucleic Acids Res 28(3);762-9. PMID: 10637328

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Grodick14: Grodick MA, Segal HM, Zwang TJ, Barton JK (2014). "DNA-Mediated Signaling by Proteins with 4Fe-4S Clusters Is Necessary for Genomic Integrity." J Am Chem Soc 136(17);6470-8. PMID: 24738733

Harrison98: Harrison L, Hatahet Z, Purmal AA, Wallace SS (1998). "Multiply damaged sites in DNA: interactions with Escherichia coli endonucleases III and VIII." Nucleic Acids Res 26(4);932-41. PMID: 9461450

Hatahet94: Hatahet Z, Kow YW, Purmal AA, Cunningham RP, Wallace SS (1994). "New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase." J Biol Chem 269(29);18814-20. PMID: 8034633

Hazra01: Hazra TK, Muller JG, Manuel RC, Burrows CJ, Lloyd RS, Mitra S (2001). "Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli." Nucleic Acids Res 29(9);1967-74. PMID: 11328881

Hori03: Hori M, Yonei S, Sugiyama H, Kino K, Yamamoto K, Zhang QM (2003). "Identification of high excision capacity for 5-hydroxymethyluracil mispaired with guanine in DNA of Escherichia coli MutM, Nei and Nth DNA glycosylases." Nucleic Acids Res 31(4);1191-6. PMID: 12582238

Janion03: Janion C, Sikora A, Nowosielska A, Grzesiuk E (2003). "E. coli BW535, a triple mutant for the DNA repair genes xth, nth, and nfo, chronically induces the SOS response." Environ Mol Mutagen 41(4);237-42. PMID: 12717778

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

Jurado98: Jurado J, Saparbaev M, Matray TJ, Greenberg MM, Laval J (1998). "The ring fragmentation product of thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins." Biochemistry 37(21);7757-63. PMID: 9601036

Kim88: Kim J, Linn S (1988). "The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites." Nucleic Acids Res 16(3);1135-41. PMID: 2449657

Kroeger03: Kroeger KM, Hashimoto M, Kow YW, Greenberg MM (2003). "Cross-linking of 2-deoxyribonolactone and its beta-elimination product by base excision repair enzymes." Biochemistry 42(8);2449-55. PMID: 12600212

Kuo92: Kuo CF, McRee DE, Fisher CL, O'Handley SF, Cunningham RP, Tainer JA (1992). "Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III." Science 258(5081);434-40. PMID: 1411536

Kuznetsov15: Kuznetsov NA, Kladova OA, Kuznetsova AA, Ishchenko AA, Saparbaev MK, Zharkov DO, Fedorova OS (2015). "Conformational Dynamics of DNA Repair by Escherichia coli Endonuclease III." J Biol Chem. PMID: 25869130

Lee14b: Lee AJ, Warshaw DM, Wallace SS (2014). "Insights into the glycosylase search for damage from single-molecule fluorescence microscopy." DNA Repair (Amst) 20;23-31. PMID: 24560296

Lomax05: Lomax ME, Salje H, Cunniffe S, O'Neill P (2005). "8-OxoA inhibits the incision of an AP site by the DNA glycosylases Fpg, Nth and the AP endonuclease HAP1." Radiat Res 163(1);79-84. PMID: 15606310

Lukianova05: Lukianova OA, David SS (2005). "A role for iron-sulfur clusters in DNA repair." Curr Opin Chem Biol 9(2);145-51. PMID: 15811798

Matsumoto01: Matsumoto Y, Zhang QM, Takao M, Yasui A, Yonei S (2001). "Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA." Nucleic Acids Res 29(9);1975-81. PMID: 11328882

Mazumder91: Mazumder A, Gerlt JA, Absalon MJ, Stubbe J, Cunningham RP, Withka J, Bolton PH (1991). "Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys." Biochemistry 30(4);1119-26. PMID: 1846560

Miller04: Miller H, Fernandes AS, Zaika E, McTigue MM, Torres MC, Wente M, Iden CR, Grollman AP (2004). "Stereoselective excision of thymine glycol from oxidatively damaged DNA." Nucleic Acids Res 32(1);338-45. PMID: 14726482

Mol00: Mol CD, Hosfield DJ, Tainer JA (2000). "Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means." Mutat Res 460(3-4);211-29. PMID: 10946230

Nelson14: Nelson SR, Dunn AR, Kathe SD, Warshaw DM, Wallace SS (2014). "Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases." Proc Natl Acad Sci U S A 111(20);E2091-9. PMID: 24799677

Piersen00: Piersen CE, McCullough AK, Lloyd RS (2000). "AP lyases and dRPases: commonality of mechanism." Mutat Res 459(1);43-53. PMID: 10677682

Purmal98: Purmal AA, Lampman GW, Bond JP, Hatahet Z, Wallace SS (1998). "Enzymatic processing of uracil glycol, a major oxidative product of DNA cytosine." J Biol Chem 273(16);10026-35. PMID: 9545349

Radman76: Radman M (1976). "An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA." J Biol Chem 251(5);1438-45. PMID: 3498

Romano11: Romano CA, Sontz PA, Barton JK (2011). "Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a first step in lesion detection." Biochemistry 50(27);6133-45. PMID: 21651304

Saito97a: Saito Y, Uraki F, Nakajima S, Asaeda A, Ono K, Kubo K, Yamamoto K (1997). "Characterization of endonuclease III (nth) and endonuclease VIII (nei) mutants of Escherichia coli K-12." J Bacteriol 179(11);3783-5. PMID: 9171430

Serafini99: Serafini DM, Schellhorn HE (1999). "Endonuclease III and endonuclease IV protect Escherichia coli from the lethal and mutagenic effects of near-UV irradiation." Can J Microbiol 45(7);632-7. PMID: 10497792

Sontz12: Sontz PA, Mui TP, Fuss JO, Tainer JA, Barton JK (2012). "DNA charge transport as a first step in coordinating the detection of lesions by repair proteins." Proc Natl Acad Sci U S A 109(6);1856-61. PMID: 22308447

Suzuki08: Suzuki T, Yamamoto K, Harashima H, Kamiya H (2008). "Base excision repair enzyme endonuclease III suppresses mutagenesis caused by 8-hydroxy-dGTP." DNA Repair (Amst) 7(1);88-94. PMID: 17870674

Tano01: Tano K, Iwamatsu Y, Yasuhira S, Utsumi H, Takimoto K (2001). "Increased base change mutations at G:C pairs in Escherichia coli deficient in endonuclease III and VIII." J Radiat Res 42(4);409-13. PMID: 11951664

Thayer95: Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA (1995). "Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure." EMBO J 14(16);4108-20. PMID: 7664751

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

Wagner96: Wagner JR, Blount BC, Weinfeld M (1996). "Excision of oxidative cytosine modifications from gamma-irradiated DNA by Escherichia coli endonuclease III and human whole-cell extracts." Anal Biochem 233(1);76-86. PMID: 8789150

Warner80: Warner HR, Demple BF, Deutsch WA, Kane CM, Linn S (1980). "Apurinic/apyrimidinic endonucleases in repair of pyrimidine dimers and other lesions in DNA." Proc Natl Acad Sci U S A 77(8);4602-6. PMID: 6254032

Watanabe05: Watanabe T, Blaisdell JO, Wallace SS, Bond JP (2005). "Engineering functional changes in Escherichia coli endonuclease III based on phylogenetic and structural analyses." J Biol Chem 280(40);34378-84. PMID: 16096281

Weiss85: Weiss B, Cunningham RP (1985). "Genetic mapping of nth, a gene affecting endonuclease III (thymine glycol-DNA glycosylase) in Escherichia coli K-12." J Bacteriol 162(2);607-10. PMID: 3886628

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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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