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Information on EC 3.1.26.3 - ribonuclease III and Organism(s) Escherichia coli and UniProt Accession P0A7Y0

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.3 ribonuclease III
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Escherichia coli
UNIPROT: P0A7Y0 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
dicer, dicer1, drosha, dicer-2, rnt1p, ribonuclease iii, dicer-1, rnase d, dcr-1, rnase3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonuclease III
-
E. coli RNase III
-
-
endoribonuclease III
-
-
HCS protein
-
-
-
-
nuclease, ribo-, D
-
-
-
-
p241
-
-
-
-
ribonuclease D
-
-
-
-
ribonuclease III
RNase D
-
-
-
-
RNase III
RNase O
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to a 5'-phosphomonoester
show the reaction diagram
mechanism of RNase III catalytic action, overview. Endoribonucleolytic activity of RNase III produces 2-nucleotide 3'-OH overhang at the end of dsRNA substrates
Endonucleolytic cleavage to a 5'-phosphomonoester
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric diester
-
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric diester
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
78413-14-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
R1.1 RNA + H2O
?
show the reaction diagram
internally 32P-labeled R1.1
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
double-stranded RNA + H2O
?
show the reaction diagram
-
R1.1 RNA
-
-
?
ds-rRNA + H2O
mature ds-rRNA
show the reaction diagram
dsRNA + H2O
?
show the reaction diagram
-
RNase III(E38A) generates discrete-sized products from long dsRNA
-
-
?
dsRNA + H2O
mature RNA
show the reaction diagram
dsRNA + H2O
processed RNA
show the reaction diagram
hairpin RNA R1.1 + H2O
?
show the reaction diagram
-
RNase III(E38A) cleaves at the primary site and remains bound to the RNA, thereby preventing cleavage at the secondary site
-
-
?
mRNA transcripts + H2O
5'-phosphooligonucleotides
show the reaction diagram
poly(A)-poly(U) + H2O
5'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
pre-16S rRNA + H2O
mature 16S rRNA
show the reaction diagram
-
-
-
-
?
pre-23S rRNA + H2O
mature 23S rRNA
show the reaction diagram
-
-
-
-
?
pre-5S rRNA + H2O
mature 5S rRNA
show the reaction diagram
-
-
-
-
?
pre-mRNA + H2O
mature mRNA
show the reaction diagram
pre-rRNA + H2O
mature rRNA
show the reaction diagram
-
-
-
-
?
R1.1 RNA + H2O
2 fragment of R1.1 RNA
show the reaction diagram
-
substrate is enzymatically synthesized based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, 1 cleavage site
-
-
?
R1.1 RNA + H2O
2 fragments of R1.1 RNA
show the reaction diagram
R1.1 RNA + H2O
?
show the reaction diagram
-
-
-
-
?
R1.1 RNA + H2O
fragments of R1.1 RNA
show the reaction diagram
R1.1 RNA derivatives + H2O
fragments of R1.1 RNA
show the reaction diagram
-
based on the R1.1 processing signal, which is encoded in the phage T7 genetic early region between genes 1.0 and 1.1, derivative R1.1[CL3B] is not cleaved and its binding to the enzyme leads to uncoupling of substrate recognition and cleavage
-
-
?
ribosomal RNA + H2O
smaller precursor rRNA
show the reaction diagram
RNA + H2O
?
show the reaction diagram
-
-
-
-
?
RNA precursor + H2O
mature RNA
show the reaction diagram
-
phage lambda RNA, enzyme is involved in translation control
-
-
?
RNA substituted with guanosine 5'-O-(1-thiotriphosphate) + H2O
5'-phosphooligonucleotides containing guanosine 5'-O-(1-thiotriphosphate)
show the reaction diagram
-
cleavage specificity is not altered by modified RNA
-
-
?
single-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
tRNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
-
cleaves multimeric tRNA precursor at the spacer region, also involved in processing of precursor rRNA, hnRNA and early T7-mRNA. Also cleaves double-stranded DNA and single-stranded RNA
-
-
?
ds-rRNA + H2O
mature ds-rRNA
show the reaction diagram
-
-
-
-
?
dsRNA + H2O
mature RNA
show the reaction diagram
dsRNA + H2O
processed RNA
show the reaction diagram
-
-
-
-
?
pre-16S rRNA + H2O
mature 16S rRNA
show the reaction diagram
-
-
-
-
?
pre-23S rRNA + H2O
mature 23S rRNA
show the reaction diagram
-
-
-
-
?
pre-5S rRNA + H2O
mature 5S rRNA
show the reaction diagram
-
-
-
-
?
pre-mRNA + H2O
mature mRNA
show the reaction diagram
-
enzyme regulates gene expression by controlling mRNA translation and stability
-
-
?
pre-rRNA + H2O
mature rRNA
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
inhibits Mg2+ dependent reaction
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyisoquinoline-1,3-dione
-
inhibits cleavage of R1.1 RNA, IC50: 0.014 mM for Mg2+-supported reaction, 0.008 mM for Mn2+-suppoeted reaction, noncompetitive inhibition
2-mercaptoethanol
-
required
Double-stranded RNA
-
inhibits cleavage of single-stranded RNA
-
Ethidium bromide
F-
-
inhibits at 100 mM
inhibitory base pair sequences within a RNA substrate
-
inclusion of disfavored base pair sequences inhibit activity
-
KCl
-
enzyme is sensitive to high salt conditions, above 50 mM, the mutant homodimer and the heterodimer are more sensitive than the wild-type
poly(IC)
-
as double-stranded RNA
-
tRNA
-
inhibits enzyme activity and inhibition by ethidium bromide
YmdB
-
stress-responsive ribonuclease-binding regulator of Escherichia coli RNase III activity. Interacting with a site in the RNase III catalytic region. Expression of YmdB is transcriptionally activated by both cold-shock stress and the entry of cells into stationary phase, and that this activation requires the delta-factor-encoding gene, rpoS
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
less than 1 mM
glutamate
-
extends salt concentration range
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000163 - 0.000239
R1.1 RNA
-
38
Mn2+
-
mutant E117D, pH 7.5, 37°C
0.000041 - 0.003
R1.1 RNA
-
0.00026 - 0.34
RNA
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0057 - 0.029
R1.1 RNA
-
0.00035 - 0.72
R1.1 RNA
-
3.8 - 7.7
RNA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23.85 - 177.9
R1.1 RNA
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
Ethidium bromide
-
pH 8.0, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
2-hydroxyisoquinoline-1,3-dione
Escherichia coli
-
inhibits cleavage of R1.1 RNA, IC50: 0.014 mM for Mg2+-supported reaction, 0.008 mM for Mn2+-suppoeted reaction, noncompetitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
gel mobility shift assay for substrate bindng determination
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.2
-
-
7 - 7.4
-
inactive below, RNA
7.5
-
assay at
7.9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 7.4
-
-
7.6 - 9.75
-
-
8 - 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
-
-
30 - 45
-
no activity at 0°C and 17.5°C
additional information
-
samples of bacterial cultures are grown in LB medium at 28°C or 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
RNase III is a member of the phylogenetically highly conserved endoribonuclease III family
malfunction
metabolism
physiological function
evolution
malfunction
metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
-
recombinant GST-tagged wild-type homodimer, gel filtration
25600
29000
40000 - 55000
41000
-
RNase O, gel filtration
54000
-
recombinant His-tagged mutant homodimer, gel filtration
78000
-
recombinant His-tagged and GST-tagged wild-type/mutant heterodimer, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
the RNase III polypeptide (~220 amino acids) consists of an N-terminal catalytic domain [RIIID, about 150 amino acids (aa)] and a C-terminal dsRNA-binding domain (dsRBD, about 65 aa) joined by a short (10 aa) flexible linker. The active form of the enzyme is a homodimer, with a functionally independent catalytic site in each subunit and two dsRBDs that assist in substrate binding
?
-
x * 25600, amino acid sequence calculation, x * 29000, recombinant His-tagged enzyme, SDS-PAGE
dimer
heterodimer
-
preparation of artificial heterodimers of RNase III, which are providing new insight on the subunit and domain interactions involved in dsRNA recognition and cleavage
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphoprotein
-
phosphorylation on a serine in the RNase III domain activates the enzyme, the covalent modification facilitates product release, which is the rate-limiting step in the catalytic pathway
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
12 three-dimensional structures of bacterial RNase III in various forms have been reported
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D128A
site-directed mutagenesis, the D128A mutation in both RNase III subunits, D128A/D128'A, causes an 83fold increase in KD in the interaction of RNase III with YmdB
Q153P
the Q153P substitution in the middle of the flexible linker between the endoND and the dsRBD abolish RNA-cleavage activity
S195A/S198A
site-directed mutagenesis, the mutant shows a slightly reduced phosphorylation level compared to wild-type
S33E/S34E
site-directed mutagenesis of phosphorylation sites, molecular dynamic simulations of the S33E/S34E double mutant, which formally provides the same double-negative charge as a single S33 or S34 phosphomonoester, indicate that an additional acidic residue at position 34 does not provide a stabilized interaction with R95. In contrast to the bidentate pS33-R95 side chain interaction, the observed salt bridge consists of a monodentate engagement of R95 with the E33 side chain, and no involvement of the E34 side chain. The S33E/S34E mutant shows abolished phosphorylation and cleaves R1.1 RNA with an efficiency comparable to, but not greater than unphosphorylated RNase III. The S33A/S34A double mutant is essentially fully resistant to phosphorylation
D114A
-
mutant exhibits catalytic activity in vitro in 10 mM Mg2+ buffer that is comparable to that of the wild-type enzyme. At 1 mM Mg2+, the activity is significantly lower, KM-value for Mg2+ is about 2.8fold larger than the wild-type value
D45A
-
mutant enzyme exhibits negligible activity, regardless of the Mg2+ concentration
D45N
-
mutant enzyme exhibits negligible activity, regardless of the Mg2+ concentration
E100A
-
mutant enzyme requires higher Mg2+ concentrations for optimal activity than the wild-type enzyme
E117D
-
site-directed mutagenesis, mutant exhibits normal homodimeric behaviour, can bind substrates but shows highly reduced hydrolysis activity compared to the wild-type enzyme
E117Q
E41A
-
mutant exhibits catalytic activity in vitro in 10 mM Mg2+ buffer that is comparable to that of the wild-type enzyme. At 1 mM Mg2+, the activity is significantly lower, KM-value for Mg2+ is about 2.8fold larger than the wild-type value
E41A/D114A
-
KM-value for Mg2+ is about 85fold larger than the wild-type value
E65A
-
mutant enzyme requires higher Mg2+ concentrations for optimal activity than the wild-type enzyme
G97E
-
increases requirement for Mg2+
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
nonspecific cleavage of RNA after heating for 1 min
37
-
30 min, no loss af activity
50
-
30 min, 50% loss af activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM Tris, pH 8, 8% (NH4)2SO4, 50% glycerol, several months, no loss of activity
-
-70°C, 1.3 M NH4Cl, 2 years, 40-50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)recA,rnc105 by nickel affinity chromatography, the tag is cleaved off by thrombin
affinity chromatography. RNase III heterodimers also can be purified from the inclusion body
-
of the overexpressed protein
-
of the overexpressed protein in yeast
-
partially RNase O
-
recombinant His-tagged enzyme to over 90% purity
-
recombinant His-tagged RNase III from Escherichia coli by nickel affinity chromatography
-
recombinant HIs-tagged wild-type and mutant enzymes
-
recombinant hybrid proteins to homogeneity
-
recombinant mutant enzymes
-
recombinant tagged heterodimer and homodimers from strain BL21 to homogeneity
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rnc, phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)recA,rnc105
analysis of the rnd gene in Escherichia coli
-
expressed in Escherichia coli BLR(DE3) cells
-
expression of a His-tagged E117Q mutant homodimer, a GST-tagged wild-type homodimer, and a His-tagged and GST-tagged wild-type/mutant heterodimer in strain BL21
-
gene rnc, expression of wild-type and mutant enzymes in strain BL21(DE3) as His-tagged enzymes
-
gene rnc, mapping at 55 min on the bacterial chromosome, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene rnc, overexpression of wild-type and mutants in strain BL21(DE3) as His-tagged proteins
-
mutant proteins expressed in Escherichia coli
-
overexpression in Saccharomyces cerevisiae
-
overexpression of mutant hybrid proteins in Escherichia coli strain HMS174
-
overexpression of the rnc gene in Escherichia coli
-
recombinant expression of His-tagged RNase III in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the RNase III operon includes the rnc and era genes encoding RNase III and Era proteins, respectively. RNase III cleaves its own leader RNA, causing instability of its mRNA. Thus, RNase III can repress its own synthesis and also that of Era, because era is transcriptionally and translationally coupled to rnc expression. Era function is critical for maintaining cell growth and cell division rate in Escherichia coli, so that the regulation of Era levels by RNase III has been proposed as an important feature of the Escherichia coli cell cycle
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, S.M.; Takiff, H.E.; Barber, A.M.; Dubois, G.C.; Bardwell, J.C.A.; Court, D.L.
Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli
J. Biol. Chem.
265
2888-2895
1990
Escherichia coli
Manually annotated by BRENDA team
Nicholson, A.W.; Niebling, K.R.; McOsker, P.L.; Robertson, H.D.
Accurate in vitro cleavage by RNase III of phosphorothioate-substituted RNA processing signals in bacteriophage T7 early mRNA
Nucleic Acids Res.
16
1577-1591
1988
Escherichia coli
Manually annotated by BRENDA team
Gross, G.; Dunn, J.J.
Structure of secondary cleavage sites of E. coli RNAaseIII in A3t RNA from bacteriophage T7
Nucleic Acids Res.
15
431-442
1987
Escherichia coli
Manually annotated by BRENDA team
Gurevitz, M.; Apirion, D.
The ribonuclease-III-processing site near the 5 end of an RNA precursor of bacteriophage T4 and its effect on termination
Eur. J. Biochem.
147
581-586
1985
Escherichia coli
Manually annotated by BRENDA team
Watson, N.; Apirion, D.
Molecular cloning of the gene for the RNA-processing enzyme RNase III of Escherichia coli
Proc. Natl. Acad. Sci. USA
82
849-853
1985
Escherichia coli
Manually annotated by BRENDA team
Szeberenyi, J.; Roy, M.K.; Vaidya, H.C.; Apirion, D.
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
2952-2957
1984
Escherichia coli
Manually annotated by BRENDA team
King, T.C.; Sirdeshmukh, R.; Schlessinger, D.
RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA
Proc. Natl. Acad. Sci. USA
81
185-188
1984
Escherichia coli
Manually annotated by BRENDA team
Panganiban, A.T.; Whiteley, H.R.
Bacillus subtilis RNAase III cleavage sites in phage SP82 early mRNA
Cell
33
907-913
1983
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Barkay, T.; Goldfarb, A.
Processing of bacteriophage T4 primary transcripts with ribonuclease III
J. Mol. Biol.
162
299-315
1982
Escherichia coli
Manually annotated by BRENDA team
Dunn, J.J
Ribonuclease III
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
15
485-499
1982
Bos taurus, Escherichia coli, Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Birenbaum, M.; Shen, V.; Nikolaev, N.; Schlessinger, D.
Site-specific processing of Escherichia coli preribosomal RNA and preribosomes by E. coli RNase III
Methods Enzymol.
59
824-837
1979
Escherichia coli
Manually annotated by BRENDA team
Shimura, Y.; Sakano, H.; Nagawa, F.
Specific ribonucleases involved in processing of tRNA precursors of Escherichia coli. Partial purification and some properties
Eur. J. Biochem.
86
267-281
1978
Escherichia coli
Manually annotated by BRENDA team
Dunn, J.J.
RNase III cleavage of single-stranded RNA. Effect of ionic strength on the fideltiy of cleavage
J. Biol. Chem.
251
3807-3814
1976
Escherichia coli
Manually annotated by BRENDA team
Paddock, G.V.; Fukada, K.; Abelson, J.; Robertson, H.D.
Cleavage of T4 species I ribonucleic acid by Escherichia coli ribonuclease III
Nucleic Acids Res.
3
1351-1371
1976
Escherichia coli
Manually annotated by BRENDA team
Crouch, R.J.
Ribonuclease 3 does not degrade deoxyribonucleic acid-ribonucleic acid hybrids
J. Biol. Chem.
249
1314-1316
1974
Escherichia coli
Manually annotated by BRENDA team
Robertson, H.D.; Webster, R.E.; Zinder, N.D.
Purification and properties of ribonuclease III from Escherichia coli
J. Biol. Chem.
243
82-91
1968
Escherichia coli
Manually annotated by BRENDA team
Zhang, J.R.; Deutscher, M.P.
Analysis of the upstream region of the Escherichia coli rnd gene encoding RNase D. Evidence for translational regulation of a putative tRNA processing enzyme
J. Biol. Chem.
264
18228-18233
1989
Escherichia coli
Manually annotated by BRENDA team
Srivastava, R.A.; Srivastava, N.; Apirion, D.
RNA processing enzymes RNase III, E and P in Escherichia coli are not ribosomal enzymes
Biochem. Int.
25
57-65
1991
Escherichia coli
Manually annotated by BRENDA team
Srivastava, R.A.; Srivastava, N.; Apirion, D.
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
737-749
1992
Escherichia coli
Manually annotated by BRENDA team
Li, H.L.; Chelladurai, B.S.; Zhang, K.; Nicholson, A.W.
Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects
Nucleic Acids Res.
21
1919-1925
1993
Escherichia coli
Manually annotated by BRENDA team
Davidov, Y.; Rahat, A.; Flechner, I.; Pines, O.
Characterization of the rnc-97 mutation of RNAaseIII: a glycine to glutamate substitution increases the requirement for magnesium ions
J. Gen. Microbiol.
139
717-724
1993
Escherichia coli
Manually annotated by BRENDA team
Srivastava, R.A.; Srivastava, N.
The multifaceted roles of the RNA processing enzyme ribonuclease III
Indian J. Biochem. Biophys.
33
253-260
1996
Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Srivastava, N.; Srivastava, R.A.
Expression, purification and properties of recombinant E. coli ribonuclease III
Biochem. Mol. Biol. Int.
39
171-180
1996
Escherichia coli
Manually annotated by BRENDA team
Zhang, K.; Nicholson, A.W.
Regulation of ribonuclease III processing by double-helical sequence antideterminants
Proc. Natl. Acad. Sci. USA
94
13437-13441
1997
Escherichia coli
Manually annotated by BRENDA team
Conrad, C.; Rauhut, R.; Klug, G.
Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli
Nucleic Acids Res.
26
4446-4453
1998
Escherichia coli, Rhodobacter capsulatus
Manually annotated by BRENDA team
Binnie, U.; Wong, K.; McAteer, S.; Masters, M.
Absence of RNASE III alters the pathway by which RNAI, the antisense inhibitor of ColE1 replication, decays
Microbiology
145
3089-3100
1999
Escherichia coli
Manually annotated by BRENDA team
Sun, W.; Nicholson, A.W.
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
5102-5110
2001
Escherichia coli
Manually annotated by BRENDA team
Sun, W.; Jun, E.; Nicholson, A.W.
Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain
Biochemistry
40
14976-14984
2001
Escherichia coli
Manually annotated by BRENDA team
Calin-Jageman, I.; Nicholson, A.W.
Mutational analysis of an RNA internal loop as a reactivity epitope for Escherichia coli ribonuclease III substrates
Biochemistry
42
5025-5034
2003
Escherichia coli
Manually annotated by BRENDA team
Conrad, C.; Evguenieva-Hackenberg, E.; Klug, G.
Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III
FEBS Lett.
509
53-58
2001
Escherichia coli, Rhodobacter capsulatus
Manually annotated by BRENDA team
Conrad, C.; Schmitt, J.G.; Evguenieva-Hackenberg, E.; Klug, G.
One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers
FEBS Lett.
518
93-96
2002
Escherichia coli
Manually annotated by BRENDA team
Amarasinghe, A.K.; Calin-Jageman, I.; Harmouch, A.; Sun, W.; Nicholson, A.W.
Escherichia coli ribonuclease III: affinity purification of hexahistidine-tagged enzyme and assays for substrate binding and cleavage
Methods Enzymol.
342
143-158
2001
Escherichia coli
Manually annotated by BRENDA team
Zamore, P.D.
Thirty-three years later, a glimpse at the ribonuclease III active site
Mol. Cell
8
1158-1160
2001
Aquifex aeolicus, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Calin-Jageman, I.; Amarasinghe, A.K.; Nicholson, A.W.
Ethidium-dependent uncoupling of substrate binding and cleavage by Escherichia coli ribonuclease III
Nucleic Acids Res.
29
1915-1925
2001
Escherichia coli
Manually annotated by BRENDA team
Calin-Jageman, I.; Nicholson, A.W.
RNA structure-dependent uncoupling of substrate recognition and cleavage by Escherichia coli ribonuclease III
Nucleic Acids Res.
31
2381-2392
2003
Escherichia coli
Manually annotated by BRENDA team
Sun, W.; Li, G.; Nicholson, A.W.
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
13054-13062
2004
Escherichia coli
Manually annotated by BRENDA team
Zhang, H.; Kolb, F.A.; Jaskiewicz, L.; Westhof, E.; Filipowicz, W.
Single processing center models for human Dicer and bacterial RNase III
Cell
118
57-68
2004
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Sun, W.; Pertzev, A.; Nicholson, A.W.
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
807-815
2005
Escherichia coli
Manually annotated by BRENDA team
Ji, X.
Structural basis for non-catalytic and catalytic activities of ribonuclease III
Acta Crystallogr. Sect. D
62
933-940
2006
Thermotoga maritima, Aquifex aeolicus (O67082), Escherichia coli (P0A7Y0), Saccharomyces cerevisiae (Q02555), Homo sapiens (Q9NRR4), Homo sapiens (Q9UPY3)
Manually annotated by BRENDA team
MacRae, I.J.; Doudna, J.A.
Ribonuclease revisited: structural insights into ribonuclease III family enzymes
Curr. Opin. Struct. Biol.
17
138-145
2007
Aquifex aeolicus, Saccharomyces cerevisiae, Escherichia coli, Giardia intestinalis, Homo sapiens
Manually annotated by BRENDA team
Kim, K.S.; Manasherob, R.; Cohen, S.N.
YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity
Genes Dev.
22
3497-3508
2008
Escherichia coli
Manually annotated by BRENDA team
Meng, W.; Nicholson, R.H.; Nathania, L.; Pertzev, A.V.; Nicholson, A.W.
New approaches to understanding double-stranded RNA processing by ribonuclease III purification and assays of homodimeric and heterodimeric forms of RNase III from bacterial extremophiles and mesophiles
Methods Enzymol.
447
119-129
2008
Escherichia coli, Aquifex aeolicus (O67082), Aquifex aeolicus, Thermotoga maritima (Q9X0I6), Thermotoga maritima
Manually annotated by BRENDA team
Resch, A.; Afonyushkin, T.; Lombo, T.B.; McDowall, K.J.; Blaesi, U.; Kaberdin, V.R.
Translational activation by the noncoding RNA DsrA involves alternative RNase III processing in the rpoS 5-leader
RNA
14
454-459
2008
Escherichia coli
Manually annotated by BRENDA team
Xiao, J.; Feehery, C.E.; Tzertzinis, G.; Maina, C.V.
E. coli RNase III(E38A) generates discrete-sized products from long dsRNA
RNA
15
984-991
2009
Escherichia coli
Manually annotated by BRENDA team
Kim, K.; Sim, S.H.; Jeon, C.O.; Lee, Y.; Lee, K.
Base substitutions at scissile bond sites are sufficient to alter RNA-binding and cleavage activity of RNase III
FEMS Microbiol. Lett.
315
30-37
2011
Escherichia coli
Manually annotated by BRENDA team
Opdyke, J.A.; Fozo, E.M.; Hemm, M.R.; Storz, G.
RNase III participates in GadY-dependent cleavage of the gadX-gadW mRNA
J. Mol. Biol.
406
29-43
2011
Escherichia coli
Manually annotated by BRENDA team
Lim, B.; Ahn, S.; Sim, M.; Lee, K.
RNase III controls mltD mRNA degradation in Escherichia coli
Curr. Microbiol.
68
518-523
2014
Escherichia coli, Escherichia coli HT115
Manually annotated by BRENDA team
Lim, B.; Sim, S.H.; Sim, M.; Kim, K.; Jeon, C.O.; Lee, Y.; Ha, N.C.; Lee, K.
RNase III controls the degradation of corA mRNA in Escherichia coli
J. Bacteriol.
194
2214-2220
2012
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Johanson, T.M.; Lew, A.M.; Chong, M.M.
MicroRNA-independent roles of the RNase III enzymes Drosha and Dicer
Open Biology
3
130144
2013
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Sim, M.; Lim, B.; Sim, S.H.; Kim, D.; Jung, E.; Lee, Y.; Lee, K.
Two tandem RNase III cleavage sites determine betT mRNA stability in response to osmotic stress in Escherichia coli
PLoS ONE
9
e100520
2014
Escherichia coli, Escherichia coli MG1655rnc
Manually annotated by BRENDA team
Kavalchuk, K.; Madhusudan, S.; Schnetz, K.
RNase III initiates rapid degradation of proU mRNA upon hypo-osmotic stress in Escherichia coli
RNA Biol.
9
98-109
2012
Escherichia coli
Manually annotated by BRENDA team
Malagon, F.
RNase III is required for localization to the nucleoid of the 5 pre-rRNA leader and for optimal induction of rRNA synthesis in E. coli
RNA
19
1200-1207
2013
Escherichia coli (B1XB41)
Manually annotated by BRENDA team
Nicholson, A.W.
Ribonuclease III mechanisms of double-stranded RNA cleavage
Wiley Interdiscip. Rev. RNA
5
31-48
2013
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Schizosaccharomyces pombe, Giardia intestinalis (A8BQJ3), Aquifex aeolicus (O67082), Mycobacterium tuberculosis (P9WH03), Thermotoga maritima (Q9X0I6), Mycobacterium tuberculosis H37Rv (P9WH03)
Manually annotated by BRENDA team
Carzaniga, T.; Deho, G.; Briani, F.
RNase III-independent autogenous regulation of Escherichia coli polynucleotide phosphorylase via translational repression
J. Bacteriol.
197
1931-1938
2015
Escherichia coli (P0A7Y0)
Manually annotated by BRENDA team
Lim, B.; Sim, M.; Lee, H.; Hyun, S.; Lee, Y.; Hahn, Y.; Shin, E.; Lee, K.
Regulation of Escherichia coli RNase III activity
J. Microbiol.
53
487-494
2015
Aquifex aeolicus (O67082), Escherichia coli (P0A7Y0), Escherichia coli
Manually annotated by BRENDA team
Gordon, G.; Cameron, J.; Pfleger, B.
RNA sequencing identifies new RNase III cleavage sites in Escherichia coli and reveals increased regulation of mRNA
mBio
8
e00128-17
2017
Escherichia coli (P0A7Y0), Escherichia coli MG1693 (P0A7Y0)
Manually annotated by BRENDA team
Altuvia, Y.; Bar, A.; Reiss, N.; Karavani, E.; Argaman, L.; Margalit, H.
In vivo cleavage rules and target repertoire of RNase III in Escherichia coli
Nucleic Acids Res.
46
10380-10394
2018
Escherichia coli (P0A7Y0), Escherichia coli MG1655 (P0A7Y0)
Manually annotated by BRENDA team
Paudyal, S.; Alfonso-Prieto, M.; Carnevale, V.; Redhu, S.; Klein, M.; Nicholson, A.
Combined computational and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB
Proteins
83
459-472
2015
Escherichia coli (P0A7Y0), Escherichia coli
Manually annotated by BRENDA team
Gone, S.; Alfonso-Prieto, M.; Paudyal, S.; Nicholson, A.W.
Mechanism of ribonuclease III catalytic regulation by serine phosphorylation
Sci. Rep.
6
25448
2016
Escherichia coli (P0A7Y0), Escherichia coli
Manually annotated by BRENDA team