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



Gene: rnc Accession Numbers: EG10857 (EcoCyc), b2567, ECK2565

Synonyms: ranA

Regulation Summary Diagram: ?

Subunit composition of RNase III = [Rnc]2
         RNase III = Rnc

Summary:
RNase III is an endonuclease that cleaves double-stranded RNA to yield 5'-phosphates and 3'-hydroxyls [Robertson75]. It is required for processing of ribosomal RNA (rRNA) and phage mRNA, for the regulation of a number of genes and for proper function of regulatory antisense RNAs, usually cleaving dsRNA created by the formation of stem structures within single-stranded RNA.

RNase III is a key enzyme in rRNA processing, cleaving 30S precursor rRNA to yield 23S, 17S and 5S rRNA, though it has been suggested based on degradation experiments that the 30S RNA is not actually a precursor to these rRNAs [Ginsburg75, Nikolaev74, Gegenheimer75]. The 23S rRNA sequence is flanked by RNase III cleavage sites and is cleaved at multiple points at its 5' end and one at its 3' end [Bram80, Sirdeshmukh85a, Stark85]. Some of the 5' cleavage of 23S rRNA occurs even in the absence of RNase III [Sirdeshmukh85]. Regions flanking the 16S rRNA are predicted to form a 26-bp double helical stem at the base of a loop containing the 16S rRNA. RNase III cleaves at both sites that combine to form the stem [Young78a]. Electron microscopy confirms that both the 16S and 23S rRNA sequences form loops with stems made from flanking regions that coincide with RNase III cleavage sites [Edlind80]. 5S rRNA is seperated from the 30S precursor as a 7S fragment, which is then cleaved at its 3' end by RNase III and finally by RNase E to yield the final 5S rRNA [Szeberenyi84]. In the absence of RNase III activity, mature 16S rRNA can still be found, but no mature 23S rRNA is detectable and unprocessed 23S rRNA with extraneous sequence is incorporated in 50S ribosomes [King84]. This unprocessed 30S rRNA can contribute elements to multiple ribosomes, resulting in pairs or occasionaly trios of 50S ribosomes linked together by unprocessed rRNA [Clark84].

Many types of phage RNA require RNase III processing. RNase III limits synthesis of the lambda lysogeny protein Int, possibly due to processing at RNase III sites within the int mRNA and in the nearby sib regulatory region [Belfort80, Schindler81, Guarneros82, Plunkett89]. RNase III also cleaves the lambda early N leader RNA, removing the NUTL binding site and thus preventing negative autoregulatory binding of N protein to NUTL, resulting in a 200-fold increase in N translation [Wilson02]. RNase III processes T4 species I RNA and may be required for proper transcriptional termination as well [Paddock76]. RNase III cleaves at multiple sites within the T7 phage genome, including the initiator RNA A3t and gene 1.2, which is subject to 3' processing [Gross87, Saito81]. RNase III cleavage of T7 RNA has been extensively evaluated at the R.1 site [Li93]. Cleavage at R1.1 depends not on specific sequence information but on the asymmetry of the 4/5 loop at that site [CalinJageman03]. A mutant with a bulge-helix-bulge motif replacing this asymmetric loop is bound but not hydrolyzed by RNase III [CalinJageman03a]. RNase III processes high molecular weight T3 RNA polymerase transcripts into discrete late T3 RNAs [Majumder77]. MS2 phage RNA with an artificially-inserted RNase III stem-loop target undergoes selective pressure from RNase III, evolving variants with base mismatches, bulges and shortened stems, all of which are inviable RNase II targets [Klovins97].

Polynucleotide phosphorylase (PNP) regulation depends on RNase III. The half life of pnp mRNA increases from 1.5 minutes to from 8 to 40 minutes in the absence of RNase III, leading to an up to eleven-fold increase in the amount of pnp mRNA [Takata87, Portier87, Takata89]. Cleavage of the pnp transcript occurs in the 5' leader of the pnp mRNA, cleaving a stem-loop to leave a short 3' overhang [Regnier86, Jarrige01, Portier87, Takata89, RobertLe92]. Following 5' cleavage by RNase III, the remaining mRNA is processed by RNase E [Hajnsdorf94].

RNase III is also involved in processing quite a few other cellular mRNAs. It processes the end of the ribosomal protein-RNA polymerase rplJL-rpoBC operon [Barry80]. Deletions around an RNase III site in between rplL and rpoB in the same operon substantially reduce the translation efficiency of β mRNA, though there is no observable effect of the absence of RNase III [Dennis84]. RNase III cleaves in the leader of the secEnusG transcript and in the L12-β intercistronic region in the rplKAJLrpoBC transcript. Loss of RNase III stabilizes both mRNAs 1-2 fold without changing steady-state level, indicating a compensatory decrease in transcription [Chow94]. Variants of the rpsO mRNA that are destabilized by polyadenylation can be cleaved by RNase III. The RNase III-cleaved mRNA is no longer destabilized by polyadenylation [HaugelNielsen96]. The 10 Sa precursor RNA is processed twice by RNase III before undergoing a final processing step to become the tmRNA that places the SsrA tag on incompletely translated proteins [Srivastava90, Makarov92, Srivastava92]. RNase III cleaves the trp and lac operons and can inactivate lac α-peptide mRNA in vitro [Shen81, Shen82]. Primary transcripts of the metY-nusA-infB, rnc-era-recO and rpsO-pnp operons are all cleaved by RNase III in their 5' noncoding leader regions. All three mRNAs are degraded much more rapidly following processing [Regnier90]. RNase III cleavage of the metY-nusA-infB operon also releases the metY minor initiator tRNA [Regnier89]. RNase III cleaves the 5' untranslated region of both the rnc-era-recO and rnc-era transcripts, reducing their stability [Matsunaga96]. The second stem-loop in the untranslated region is required for this cleavage [Matsunaga96a]. Cleavage of rnc increases its degradation rate ten fold [Matsunaga97]. Three RNase III sites in the sdhCDAB-sucABCD intergenic region contribute to extreme instability of the operon transcript [Cunningham98a]. RNase III cleavage in the 5' untranslated region of the speF-potE transcript increases translational efficiency and thus enhances expression of ornithine decarboxylase [Kashiwagi94]. Translation from the -292 start site of the adhE gene, which is needed for fermentative growth on glucose, requires RNase III. This may be due to a predicted intramolecular base pairing in the 5' untranslated region which would be expected to block ribosome binding [MembrilloHernan99a, Aristarkhov96]. RNase III cleaves DicF RNA to a precursor stage that is then cleaved by RNase E to its final form as a trans-acting cell division inhibitor [Faubladier90]. Finally, bolA RNA is stabilized in the absence of RNase III [Santos97].

Some antisense RNA regulatory systems are RNase III targets. The antisense RNA-OUT, which regulates IS10 transposition by binding the transposase mRNA RNA-IN, folds into a stable stem-loop structure that is RNase III resistant unless certain point mutations are introduced [Case89]. However, RNase III cleavage is required for destabilization of RNA-IN following binding by RNA-OUT [Case90]. Synthesis of the plasmid IncFII replication protein RepA is controlled by binding of the antisense RNA CopA to the leader region of RepA mRNA (CopT). RNase III cleaves the CopA/CopT duplex, limiting RepA expression [Blomberg90]. Unpaired bases within the stem-loop in CopA reduce its suitability as a substrate for RNase III, limiting this regulatory cleavage [Hjalt95]. Unstable antisense RNAs target for RNase III cleavage truncated mRNAs from the Hok/Sok (plasmid R1), SrnB (F plasmid) and Pnd (plasmid R438) plasmid toxicity systems. Absence of the truncated mRNAs leads to rapid degradation of the stable full-length mRNAs that code for toxins [Gerdes92]. Sok antisense RNA forms a three-way junction with hok mRNA (which forms an internal stem-loop). This Sok binding, along with the presence of a transcriptional terminator hairpin within Sok, allows RNase III cleavage to occur [Franch99].

RNAI, required for replication of the plasmid ColE1, is cleaved by RNase III, with polyadenylated RNAI collecting in the absence of RNase III [Binnie99]. The plasmid R1 gene 19 is also controlled by RNase III, which cleaves within the coding region of gene 19 [Koraimann93]. The copy number of miniR6-5 but not miniF plasmids is reduced 2-fold in the absence of RNase III [Ely81].

Though RNase III is dispensible for growth, mutants lacking its activity do not grow at 45° C and are nonmotile [Takiff89, Apirion75, Apirion78a]. Suppressor mutations that cancel this temperature sensitivity have been discovered [Apirion76a]. mRNA is broken down equally quickly in cells with or without RNase III, but during carbon starvation RNA decays faster in cells lacking RNase III [Apirion76, Freire06]. In strains mutated in multiple ribonucleases, lack of RNase III led to more rapid decay of RNA generally [Babitzke93]. In mutants lacking RNase III function, β-galactosidase induction from the lac operon is twice as slow as normal and yield ten times less enzyme. In vitro, β-galactosidase RNA from the mutant is three times less competent for translation initiation [Talkad78]. Mutants in RNase III supress cold sensitive suhB mutants [Inada95].

RNase III is a dimer, though a single functional active site is sufficient for catalytic activity [Dunn76, March90, Conrad02]. The dominant-negative point mutant rnc70, which binds but does not cleave dsRNA, does not necessarily exert its negative effect on wild type through formation of mixed dimers [Dasgupta98].

RNase III has two modules, an amino-terminal 150-residue catalytic domain and a carboxy-terminal 70-residue recognition module that is homologous to other dsRNA binding domains. By NMR, RNase III has an α-β-β-β-α topology, with a three-stranded β sheet packing on two α helices [Kharrat95]. Both domains play a part in substrate specificity and cleavage site selection, though truncated RNase III lacking the RNA binding domain still cleaves small substrates in vitro and is specific for dsRNA [Conrad01, Sun01a]. Changing the interdomain spacer from nine to twenty residues has no effect on RNase III activity [Conrad01]. The RNase III catalytic module has one processing center with two mRNA cleavage sites, generating products with two nucleotide 3' overhangs [Zhang04b]. Cleavage involves incorporation of a solvent oxygen atom into the 5'-phosphate of the RNA product, making cleavage irreversible. The catalytic rate depends on the divalent metal ion used in the reaction. A two-step change in fluorescence may indicate conformational change during distinct substrate binding and catalytic steps [Campbell02a]. Experiments suggest that two magnesium ions are involved in catalysis [Sun05].

Though there are no canonical motifs for RNase III cleavage, certain base pairings are unfavorable, disrupting proper RNase III binding and thus preventing subsequent cleavage. Relative to the cleavage site, GC/CG is never seen at -5, is rarely seen at -4 and -6 and is never seen at -12. UA is never seen at -11. Addition of these unfavored base pairs in the stated locations in T7 R1.1 RNA disrupted RNase III binding. The three base-pair antideterminant sequence from tRNASec, which prevents interaction with incorrect aminoacyl-tRNA-synthetases, also disrupts RNase III binding when placed in the critical -5 and -12 positions, but not when placed in the intervening region [Zhang97b]. RNase III cleavage does not depend on tertiary RNA-RNA interactions or a conserved CUU/GAA base pair sequence [Chelladurai91]. RNase III recognizes RNA duplexes longer than eleven base pairs with little specificity [Lamontagne04]. RNase III is still able to cleave at the expected site in R1.1 RNA even when a phosphorothioate internucleotide linkage is present [Nicholson88].

RNase III activity is stimulated four-fold following infection by T7 phage. The T7 protein kinase gp0.7 PK phosphorylates RNase III at a serine, stimulating processing of T7 early and late mRNAs [Mayer83, Robertson94].

Reviews: [Nicholson13, Court13]

Citations: [Nicholson99, Srivastava96, Deutscher90, Robertson90]

Locations: cytosol, inner membrane

Map Position: [2,701,405 <- 2,702,085] (58.22 centisomes)
Length: 681 bp / 226 aa

Molecular Weight of Polypeptide: 25.55 kD (from nucleotide sequence)

pI: 7.3 [Davidov93]

Unification Links: ASAP:ABE-0008448 , CGSC:271 , DIP:DIP-48223N , EchoBASE:EB0850 , EcoGene:EG10857 , EcoliWiki:b2567 , Mint:MINT-1227120 , ModBase:P0A7Y0 , OU-Microarray:b2567 , PortEco:rnc , Pride:P0A7Y0 , Protein Model Portal:P0A7Y0 , RefSeq:NP_417062 , RegulonDB:EG10857 , SMR:P0A7Y0 , String:511145.b2567 , UniProt:P0A7Y0

Relationship Links: InterPro:IN-FAMILY:IPR000999 , InterPro:IN-FAMILY:IPR001159 , InterPro:IN-FAMILY:IPR011907 , InterPro:IN-FAMILY:IPR014720 , Panther:IN-FAMILY:PTHR11207 , Pfam:IN-FAMILY:PF00035 , Pfam:IN-FAMILY:PF00636 , Pfam:IN-FAMILY:PF14622 , Prosite:IN-FAMILY:PS00517 , Prosite:IN-FAMILY:PS50137 , Prosite:IN-FAMILY:PS50142 , Smart:IN-FAMILY:SM00358 , Smart:IN-FAMILY:SM00535

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006396 - RNA processing Inferred from experiment Inferred by computational analysis [GOA01, Robertson75]
GO:0090501 - RNA phosphodiester bond hydrolysis Inferred from experiment [Robertson75]
GO:0090502 - RNA phosphodiester bond hydrolysis, endonucleolytic Inferred by computational analysis Inferred from experiment [Robertson75, GOA06, GOA01a, GOA01]
GO:0006364 - rRNA processing Inferred by computational analysis [UniProtGOA11, GOA06]
GO:0006397 - mRNA processing Inferred by computational analysis [UniProtGOA11, GOA06]
GO:0008033 - tRNA processing Inferred by computational analysis [UniProtGOA11]
GO:0016075 - rRNA catabolic process Inferred by computational analysis [GOA01]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004525 - ribonuclease III activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Robertson75]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0004518 - nuclease activity Inferred by computational analysis [UniProtGOA11]
GO:0004519 - endonuclease activity Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0005886 - plasma membrane [Miczak91a]

MultiFun Terms: information transfer RNA related RNA degradation
metabolism degradation of macromolecules RNA

Essentiality data for rnc knockouts: ?

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

Credits:
Revised 25-May-2011 by Brito D


Enzymatic reaction of: ribonuclease (RNase III)

EC Number: 3.1.26.3

RNase III mRNA processing substrate + 2 H2O <=> RNase III processing product mRNA + 2 a single-stranded RNA

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.

Summary:
The optimum pH range is 6.9-7.4.

Cofactors or Prosthetic Groups: Mg2+ [Robertson68]

T(opt): 37 °C [BRENDA14, Srivastava92, Srivastava96a]

pH(opt): 6.8 [BRENDA14, Srivastava92], 7 [BRENDA14, Shimura78], 7.15 [Srivastava96a]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 6 -> 128
[UniProt09]
UniProt: RNase III;
Mutagenesis-Variant 38
[Sun04, UniProt12]
Alternate sequence: E → A; UniProt: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+).
Mutagenesis-Variant 40
[Blaszczyk01, UniProt12]
Alternate sequence: L → W; UniProt: No effect.
Alternate sequence: L → M; UniProt: No effect.
Alternate sequence: L → R; UniProt: Loss of activity.
Alternate sequence: L → D; UniProt: Loss of activity.
Alternate sequence: L → G; UniProt: Loss of activity.
Mutagenesis-Variant 41
[Sun04, UniProt12]
Alternate sequence: E → A; UniProt: Reduced affinity for Mg(2+), catalytic defect. 85-fold reduced affinity for Mg(2+); when associated with A-114.
Metal-Binding-Site 41
[UniProt12]
UniProt: Magnesium; Non-Experimental Qualifier: probable.
Mutagenesis-Variant 44
[Dasgupta98, Nashimoto85, UniProt12]
Alternate sequence: G → S; UniProt: In rnc-105; slower growth, loss of RNase activity.
Mutagenesis-Variant 45
[Sun04, UniProt12]
Alternate sequence: D → N; UniProt: 30000-fold reduction in catalytic efficiency, binds RNA normally. Partially rescued by Mn(2+).
Alternate sequence: D → E; UniProt: 30000-fold reduction in catalytic efficiency, binds RNA normally. Partially rescued by Mn(2+).
Alternate sequence: D → A; UniProt: 30000-fold reduction in catalytic efficiency, binds RNA normally. Partially rescued by Mn(2+).
Active-Site 45
[UniProt12]
UniProt: Non-Experimental Qualifier: potential.
Mutagenesis-Variant 65
[Sun04, UniProt12]
Alternate sequence: E → A; UniProt: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+).
Mutagenesis-Variant 100
[Sun04, UniProt12]
Alternate sequence: E → A; UniProt: Reduced affinity for Mg(2+) and RNA.
Mutagenesis-Variant 114
[Sun04, UniProt12]
Alternate sequence: D → A; UniProt: Reduced affinity for Mg(2+), no catalytic defect at 10 mM Mg(2+). 85-fold reduced affinity for Mg(2+); when associated with A-41.
Metal-Binding-Site 114
[UniProt12]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 117
[Sun01b, Dasgupta98, UniProt12]
Alternate sequence: E → Q; UniProt: Loss of RNase activity, still binds RNA.
Alternate sequence: E → K; UniProt: In rnc70; slower growth, loss of RNase activity. Dominant over wild-type. Binds ds-RNA.
Alternate sequence: E → D; UniProt: Nearly complete loss of RNase activity, still binds RNA. Partially rescued by Mn(2+).
Metal-Binding-Site 117
[UniProt12]
UniProt: Magnesium; Non-Experimental Qualifier: probable.
Active-Site 117
[UniProt12]
UniProt: Non-Experimental Qualifier: probable.
Conserved-Region 155 -> 225
[UniProt09]
UniProt: DRBM;
Sequence-Conflict 168 -> 195
[March85, UniProt10a]
Alternate sequence: HLPLPTYLVVQVRGEAHDQEFTIHCQVS → PSAAADLSGSPGTWSKRTIRNLLSTARSV; UniProt: (in Ref. 2; CAA26504);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b2567 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10857; confirmed by SwissProt match.


References

Apirion75: Apirion D, Watson N (1975). "Mapping and characterization of a mutation in Escherichia coli that reduces the level of ribonuclease III specific for double-stranded ribonucleic acid." J Bacteriol 124(1);317-24. PMID: 1100606

Apirion76: Apirion D, Neil J, Watson N (1976). "Consequences of losing ribonuclease III on the Escherichia coli cell." Mol Gen Genet 144(2);185-90. PMID: 775291

Apirion76a: Apirion D, Neil J, Watson N (1976). "Revertants from RNase III negative strains of Escherichia coli." Mol Gen Genet 149(2);201-10. PMID: 796680

Apirion78a: Apirion D, Watson N (1978). "Ribonuclease III is involved in motility of Escherichia coli." J Bacteriol 133(3);1543-5. PMID: 346582

Aristarkhov96: Aristarkhov A, Mikulskis A, Belasco JG, Lin EC (1996). "Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli." J Bacteriol 178(14);4327-32. PMID: 8763968

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

Babitzke93: Babitzke P, Granger L, Olszewski J, Kushner SR (1993). "Analysis of mRNA decay and rRNA processing in Escherichia coli multiple mutants carrying a deletion in RNase III." J Bacteriol 175(1);229-39. PMID: 8416898

Barry80: Barry G, Squires C, Squires CL (1980). "Attenuation and processing of RNA from the rplJL--rpoBC transcription unit of Escherichia coli." Proc Natl Acad Sci U S A 77(6);3331-5. PMID: 6158044

Belfort80: Belfort M (1980). "The cII-independent expression of the phage lambda int gene in RNase III-defective E. coli." Gene 11(1-2);149-55. PMID: 6254850

Binnie99: Binnie U, Wong K, McAteer S, Masters M (1999). "Absence of RNASE III alters the pathway by which RNAI, the antisense inhibitor of ColE1 replication, decays." Microbiology 145 ( Pt 11);3089-100. PMID: 10589716

Blaszczyk01: Blaszczyk J, Tropea JE, Bubunenko M, Routzahn KM, Waugh DS, Court DL, Ji X (2001). "Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage." Structure 9(12);1225-36. PMID: 11738048

Blomberg90: Blomberg P, Wagner EG, Nordstrom K (1990). "Control of replication of plasmid R1: the duplex between the antisense RNA, CopA, and its target, CopT, is processed specifically in vivo and in vitro by RNase III." EMBO J 9(7);2331-40. PMID: 1694128

Bram80: Bram RJ, Young RA, Steitz JA (1980). "The ribonuclease III site flanking 23S sequences in the 30S ribosomal precursor RNA of E. coli." Cell 19(2);393-401. PMID: 6153577

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

CalinJageman03: Calin-Jageman I, Nicholson AW (2003). "Mutational analysis of an RNA internal loop as a reactivity epitope for Escherichia coli ribonuclease III substrates." Biochemistry 42(17);5025-34. PMID: 12718545

CalinJageman03a: Calin-Jageman I, Nicholson AW (2003). "RNA structure-dependent uncoupling of substrate recognition and cleavage by Escherichia coli ribonuclease III." Nucleic Acids Res 31(9);2381-92. PMID: 12711683

Campbell02a: Campbell FE, Cassano AG, Anderson VE, Harris ME (2002). "Pre-steady-state and stopped-flow fluorescence analysis of Escherichia coli ribonuclease III: insights into mechanism and conformational changes associated with binding and catalysis." J Mol Biol 317(1);21-40. PMID: 11916377

Case89: Case CC, Roels SM, Jensen PD, Lee J, Kleckner N, Simons RW (1989). "The unusual stability of the IS10 anti-sense RNA is critical for its function and is determined by the structure of its stem-domain." EMBO J 8(13);4297-305. PMID: 2480235

Case90: Case CC, Simons EL, Simons RW (1990). "The IS10 transposase mRNA is destabilized during antisense RNA control." EMBO J 9(4);1259-66. PMID: 1691096

Chelladurai91: Chelladurai BS, Li H, Nicholson AW (1991). "A conserved sequence element in ribonuclease III processing signals is not required for accurate in vitro enzymatic cleavage." Nucleic Acids Res 19(8);1759-66. PMID: 1709490

Chen90: Chen SM, Takiff HE, Barber AM, Dubois GC, Bardwell JC, Court DL (1990). "Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli." J Biol Chem 265(5);2888-95. PMID: 2105934

Chow94: Chow J, Dennis PP (1994). "Coupling between mRNA synthesis and mRNA stability in Escherichia coli." Mol Microbiol 11(5);919-31. PMID: 7517486

Clark84: Clark MW, Lake JA (1984). "Unusual rRNA-linked complex of 50S ribosomal subunits isolated from an Escherichia coli RNase III mutant." J Bacteriol 157(3);971-4. PMID: 6199344

Conrad01: Conrad C, Evguenieva-Hackenberg E, Klug G (2001). "Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III." FEBS Lett 509(1);53-8. PMID: 11734205

Conrad02: Conrad C, Schmitt JG, Evguenieva-Hackenberg E, Klug G (2002). "One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers." FEBS Lett 518(1-3);93-6. PMID: 11997024

Court13: Court DL, Gan J, Liang YH, Shaw GX, Tropea JE, Costantino N, Waugh DS, Ji X (2013). "RNase III: Genetics and Function; Structure and Mechanism." Annu Rev Genet 47;405-31. PMID: 24274754

Cunningham98a: Cunningham L, Guest JR (1998). "Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli." Microbiology 144 ( Pt 8);2113-23. PMID: 9720032

Dasgupta98: Dasgupta S, Fernandez L, Kameyama L, Inada T, Nakamura Y, Pappas A, Court DL (1998). "Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonuclease RNase III--the effect of dsRNA binding on gene expression." Mol Microbiol 28(3);629-40. PMID: 9632264

Davidov93: Davidov Y, Rahat A, Flechner I, Pines O (1993). "Characterization of the rnc-97 mutation of RNAaseIII: a glycine to glutamate substitution increases the requirement for magnesium ions." J Gen Microbiol 139(4);717-24. PMID: 8515231

Dennis84: Dennis PP (1984). "Site specific deletions of regulatory sequences in a ribosomal protein-RNA polymerase operon in Escherichia coli. Effects on beta and beta' gene expression." J Biol Chem 259(5);3202-9. PMID: 6321499

Deutscher90: Deutscher MP (1990). "Ribonucleases active at 3' terminus of transfer RNA." Methods Enzymol 181;421-33. PMID: 2166215

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

Dunn76: Dunn JJ (1976). "RNase III cleavage of single-stranded RNA. Effect of ionic strength on the fideltiy of cleavage." J Biol Chem 251(12);3807-14. PMID: 932008

Edlind80: Edlind TD, Bassel AR (1980). "Electron microscopic mapping of secondary structures in bacterial 16S and 23S ribosomal ribonucleic acid and 30S precursor ribosomal ribonucleic acid." J Bacteriol 141(1);365-73. PMID: 6153384

Ely81: Ely S, Staudenbauer WL (1981). "Regulation of plasmid DNA synthesis: isolation and characterization of copy number mutants of miniR6-5 and miniF plasmids." Mol Gen Genet 181(1);29-35. PMID: 6261084

Faubladier90: Faubladier M, Cam K, Bouche JP (1990). "Escherichia coli cell division inhibitor DicF-RNA of the dicB operon. Evidence for its generation in vivo by transcription termination and by RNase III and RNase E-dependent processing." J Mol Biol 212(3);461-71. PMID: 1691299

Franch99: Franch T, Thisted T, Gerdes K (1999). "Ribonuclease III processing of coaxially stacked RNA helices." J Biol Chem 274(37);26572-8. PMID: 10473621

Freire06: Freire P, Amaral JD, Santos JM, Arraiano CM (2006). "Adaptation to carbon starvation: RNase III ensures normal expression levels of bolA1p mRNA and sigma(S)." Biochimie 88(3-4);341-6. PMID: 16309817

Gegenheimer75: Gegenheimer P, Apirion D (1975). "Escherichia coli ribosomal ribonucleic acids are not cut from an intact precursor molecule." J Biol Chem 250(6);2407-9. PMID: 1090620

Gerdes92: Gerdes K, Nielsen A, Thorsted P, Wagner EG (1992). "Mechanism of killer gene activation. Antisense RNA-dependent RNase III cleavage ensures rapid turn-over of the stable hok, srnB and pndA effector messenger RNAs." J Mol Biol 226(3);637-49. PMID: 1380562

Ginsburg75: Ginsburg D, Steitz JA (1975). "The 30 S ribosomal precursor RNA from Escherichia coli. A primary transcript containing 23 S, 16 S, and 5 S sequences." J Biol Chem 250(14);5647-54. PMID: 1095585

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

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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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