|Gene:||rnc||Accession Numbers: EG10857 (EcoCyc), b2567, ECK2565|
Subunit composition of
RNase III = [Rnc]2
RNase III = Rnc
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, Sirdeshmukh85, Stark85]. Some of the 5' cleavage of 23S rRNA occurs even in the absence of RNase III [Sirdeshmukh85a]. 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 [Young78]. 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 [Cunningham98]. 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 [MembrilloHernan99, 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, Apirion78]. Suppressor mutations that cancel this temperature sensitivity have been discovered [Apirion76]. 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 [Apirion76a, 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, Sun01]. 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 [Zhang04]. 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 [Campbell02]. 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 [Zhang97]. 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].
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
|Biological Process:||GO:0006396 - RNA processing
GO:0090501 - RNA phosphodiester bond hydrolysis [Robertson75]
GO:0090502 - RNA phosphodiester bond hydrolysis, endonucleolytic [Robertson75, GOA06, GOA01a, GOA01]
GO:0006364 - rRNA processing [UniProtGOA11, GOA06]
GO:0006397 - mRNA processing [UniProtGOA11, GOA06]
GO:0008033 - tRNA processing [UniProtGOA11]
GO:0016075 - rRNA catabolic process [GOA01]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis [UniProtGOA11]
|Molecular Function:||GO:0004525 - ribonuclease III activity
[GOA06, GOA01a, GOA01, Robertson75]
GO:0000166 - nucleotide binding [UniProtGOA11]
GO:0003723 - RNA binding [UniProtGOA11, GOA06, GOA01]
GO:0004518 - nuclease activity [UniProtGOA11]
GO:0004519 - endonuclease activity [UniProtGOA11]
GO:0005524 - ATP binding [UniProtGOA11]
GO:0016787 - hydrolase activity [UniProtGOA11]
GO:0019843 - rRNA binding [UniProtGOA11]
GO:0046872 - metal ion binding [UniProtGOA11]
|Cellular Component:||GO:0005829 - cytosol
[DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0005886 - plasma membrane [Miczak91]
|MultiFun Terms:||information transfer → RNA related → RNA degradation|
|metabolism → degradation of macromolecules → RNA|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 1]|
Revised 25-May-2011 by Brito D
Enzymatic reaction of: ribonuclease (RNase III)
EC Number: 220.127.116.11
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.
The optimum pH range is 6.9-7.4.
|Conserved-Region||6 -> 128|
|Conserved-Region||155 -> 225|
|Sequence-Conflict||168 -> 195|
10/20/97 Gene b2567 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10857; confirmed by SwissProt match.
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
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
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
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
Campbell02: 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
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
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
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
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
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
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
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
Guarneros82: Guarneros G, Montanez C, Hernandez T, Court D (1982). "Posttranscriptional control of bacteriophage lambda gene expression from a site distal to the gene." Proc Natl Acad Sci U S A 79(2);238-42. PMID: 6281759
Hajnsdorf94: Hajnsdorf E, Carpousis AJ, Regnier P (1994). "Nucleolytic inactivation and degradation of the RNase III processed pnp message encoding polynucleotide phosphorylase of Escherichia coli." J Mol Biol 239(4);439-54. PMID: 7516438
HaugelNielsen96: Haugel-Nielsen J, Hajnsdorf E, Regnier P (1996). "The rpsO mRNA of Escherichia coli is polyadenylated at multiple sites resulting from endonucleolytic processing and exonucleolytic degradation." EMBO J 15(12);3144-52. PMID: 8670815
Kashiwagi94: Kashiwagi K, Watanabe R, Igarashi K (1994). "Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein." Biochem Biophys Res Commun 200(1);591-7. PMID: 8166735
King84: King TC, Sirdeshmukh R, Schlessinger D (1984). "RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA." Proc Natl Acad Sci U S A 81(1);185-8. PMID: 6364133
Koraimann93: Koraimann G, Schroller C, Graus H, Angerer D, Teferle K, Hogenauer G (1993). "Expression of gene 19 of the conjugative plasmid R1 is controlled by RNase III." Mol Microbiol 9(4);717-27. PMID: 7694035
Li93: Li HL, Chelladurai BS, Zhang K, Nicholson AW (1993). "Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects." Nucleic Acids Res 21(8);1919-25. PMID: 8493105
LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532
Majumder77: Majumder HK, Bishayee S, Chakraborty PR, Maitra U (1977). "Ribonuclease III cleavage of bacteriophage T3RNA polymerase transcripts to late T3 mRNAs." Proc Natl Acad Sci U S A 74(11);4891-4. PMID: 337303
MembrilloHernan99: Membrillo-Hernandez J, Lin EC (1999). "Regulation of expression of the adhE gene, encoding ethanol oxidoreductase in Escherichia coli: transcription from a downstream promoter and regulation by fnr and RpoS." J Bacteriol 181(24);7571-9. PMID: 10601216
Nicholson88: Nicholson AW, Niebling KR, McOsker PL, Robertson HD (1988). "Accurate in vitro cleavage by RNase III of phosphorothioate-substituted RNA processing signals in bacteriophage T7 early mRNA." Nucleic Acids Res 16(4);1577-91. PMID: 3279395
Nikolaev74: Nikolaev N, Schlessinger D, Wellauer PK (1974). "30 S pre-ribosomal RNA of Escherichia coli and products of cleavage by ribonuclease III: length and molecular weight." J Mol Biol 86(4);741-7. PMID: 4610145
Plunkett89: Plunkett G, Echols H (1989). "Retroregulation of the bacteriophage lambda int gene: limited secondary degradation of the RNase III-processed transcript." J Bacteriol 171(1);588-92. PMID: 2521618
Portier87: Portier C, Dondon L, Grunberg-Manago M, Regnier P (1987). "The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5' end." EMBO J 6(7);2165-70. PMID: 3308454
Regnier86: Regnier P, Portier C (1986). "Initiation, attenuation and RNase III processing of transcripts from the Escherichia coli operon encoding ribosomal protein S15 and polynucleotide phosphorylase." J Mol Biol 187(1);23-32. PMID: 3007765
Regnier89: Regnier P, Grunberg-Manago M (1989). "Cleavage by RNase III in the transcripts of the met Y-nus-A-infB operon of Escherichia coli releases the tRNA and initiates the decay of the downstream mRNA." J Mol Biol 210(2);293-302. PMID: 2481042
Regnier90: Regnier P, Grunberg-Manago M (1990). "RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression." Biochimie 72(11);825-34. PMID: 2085545
Robertson94: Robertson ES, Aggison LA, Nicholson AW (1994). "Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli." Mol Microbiol 11(6);1045-57. PMID: 8022276
Santos97: Santos JM, Drider D, Marujo PE, Lopez P, Arraiano CM (1997). "Determinant role of E. coli RNase III in the decay of both specific and heterologous mRNAs." FEMS Microbiol Lett 157(1);31-8. PMID: 9418237
Shen81: Shen V, Cynamon M, Daugherty B, Kung H, Schlessinger D (1981). "Functional inactivation of lac alpha-peptide mRNA by a factor that purifies that Escherichia coli RNase III." J Biol Chem 256(4);1896-902. PMID: 6257691
Shimura78: Shimura Y, Sakano H, Nagawa F (1978). "Specific ribonucleases involved in processing of tRNA precursors of Escherichia coli. Partial purification and some properties." Eur J Biochem 86(1);267-81. PMID: 350582
Srivastava90: Srivastava RK, Miczak A, Apirion D (1990). "Maturation of precursor 10Sa RNA in Escherichia coli is a two-step process: the first reaction is catalyzed by RNase III in presence of Mn2+." Biochimie 72(11);791-802. PMID: 1707682
Srivastava92: Srivastava RA, Srivastava N, Apirion D (1992). "Characterization of the RNA processing enzyme RNase III from wild type and overexpressing Escherichia coli cells in processing natural RNA substrates." Int J Biochem 24(5);737-49. PMID: 1375563
Stark85: Stark MJ, Gourse RL, Jemiolo DK, Dahlberg AE (1985). "A mutation in an Escherichia coli ribosomal RNA operon that blocks the production of precursor 23 S ribosomal RNA by RNase III in vivo and in vitro." J Mol Biol 182(2);205-16. PMID: 2582139
Sun01: Sun W, Jun E, Nicholson AW (2001). "Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain." Biochemistry 40(49);14976-84. PMID: 11732918
Sun01a: Sun W, Nicholson AW (2001). "Mechanism of action of Escherichia coli ribonuclease III. Stringent chemical requirement for the glutamic acid 117 side chain and Mn2+ rescue of the Glu117Asp mutant." Biochemistry 40(16);5102-10. PMID: 11305928
Sun04: Sun W, Li G, Nicholson AW (2004). "Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III. Identification of conserved acidic residues that are important for catalytic function in vitro." Biochemistry 43(41);13054-62. PMID: 15476399
Sun05: Sun W, Pertzev A, Nicholson AW (2005). "Catalytic mechanism of Escherichia coli ribonuclease III: kinetic and inhibitor evidence for the involvement of two magnesium ions in RNA phosphodiester hydrolysis." Nucleic Acids Res 33(3);807-15. PMID: 15699182
Szeberenyi84: Szeberenyi J, Roy MK, Vaidya HC, Apirion D (1984). "7S RNA, containing 5S ribosomal RNA and the termination stem, is a specific substrate for the two RNA processing enzymes RNase III and RNase E." Biochemistry 23(13);2952-7. PMID: 6380579
Wilson02: Wilson HR, Yu D, Peters HK, Zhou JG, Court DL (2002). "The global regulator RNase III modulates translation repression by the transcription elongation factor N." EMBO J 21(15);4154-61. PMID: 12145215
Young78: Young RA, Steitz JA (1978). "Complementary sequences 1700 nucleotides apart form a ribonuclease III cleavage site in Escherichia coli ribosomal precursor RNA." Proc Natl Acad Sci U S A 75(8);3593-7. PMID: 358189
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