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Information on EC 3.1.13.1 - exoribonuclease II and Organism(s) Escherichia coli and UniProt Accession P30850

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.1 exoribonuclease II
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Escherichia coli
UNIPROT: P30850 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
rnase, exoribonuclease, rnase r, rnase ii, rrp44, rnase 2, ribonuclease r, rnaser, ribonuclease 2, exonuclease isg20, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonuclease II
-
3'-5'exoribonuclease
-
-
ribonuclease II
ribonuclease Q
-
-
-
-
RNase R
additional information
-
RNase II and RNase R are the two Escherichia coli exoribonucleases that belong to the RNase II superfamily of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-24-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oligoribonucleotide + H2O
?
show the reaction diagram
final end product of RNase II is 4-nt, whereas for RNase R it is a 2-nt fragment
-
-
?
poly(A) + H2O
5'-AMP + oligonucleotide
show the reaction diagram
35-nucleotide poly(A) chain, Tyr-313 and Glu-390 are crucial for RNA specificity of RNase II, Arg-500 residue in the active site is crucial for activity but not for RNA binding. Inside the cavity the unique specific contacts for ribose established by RNase II are those with the 2nd and 4th nucleotides from the 3'-end of the RNA molecule. These contacts are necessary and sufficient for cleavage to occur, and therefore, they seem to be responsible for the RNA specificity versus DNA in RNase II
-
-
?
A(17) + H2O
AMP + ?
show the reaction diagram
-
full-length RNase R has similar activity on both poly(A) and A(17) substrates. Full-length RNase II is 20fold more active on A(17) than full-length RNase R
-
-
?
A(4) + H2O
AMP + ?
show the reaction diagram
-
poor substrate, is degraded by RNase R 400fold more slowly than A(17)
-
-
?
dsRNA + H2O
?
show the reaction diagram
-
-
-
-
?
m-RNA + H2O
?
show the reaction diagram
-
SL9A, containing one stem-loop structure, and malE-malF operon, containing two stem-loop structures
-
-
?
mRNA + H2O
5'-phosphomononucleotide
show the reaction diagram
-
-
-
-
?
mRNA + H2O
5'-phosphomononucleotides
show the reaction diagram
mRNA + H2O
?
show the reaction diagram
-
purified RNase II is unable to directly catalyse A-site cleavage in vitro, RNase II-catalysed degradation of mRNA to the ribosome border is a prerequisite for A-site cleavage. Degrades ribosome-bound mRNA to positions +18 nucleotides downstream of the ribosomal A site
-
-
?
oligonucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
poly(A)
5'-AMP
show the reaction diagram
-
-
-
-
?
poly(A) + H2O
5'-AMP + oligo(A)
show the reaction diagram
poly(A) + H2O
5'-AMP + oligonucleotide
show the reaction diagram
-
-
-
?
poly(A) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(C)
5'-CMP
show the reaction diagram
-
-
-
-
?
poly(C) + H2O
5'-CMP + oligonucleotide
show the reaction diagram
-
-
-
?
poly(G)
5'-GMP
show the reaction diagram
-
-
-
-
?
poly(U)
5'-UMP
show the reaction diagram
-
-
-
-
?
poly(U) + H2O
5'-UMP + oligonucleotide
show the reaction diagram
-
-
-
?
polyadenosine + H2O
?
show the reaction diagram
-
-
-
-
?
poly[8-3H]adenylic acid + H2O
?
show the reaction diagram
-
linear substrate, activity below 325 UE·micro g-1
-
-
?
precursor tRNA + H2O
mature tRNA + 5'-phosphomononucleotides
show the reaction diagram
RNA
5'-phosphomononucleotides
show the reaction diagram
-
3' to 5'direction only
-
-
?
rRNA + H2O
?
show the reaction diagram
-
RNase R
-
-
?
ss RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
ss RNA oligonucleotides with chain lengths less than seven + H2O
5'-phosphomononucleotides
show the reaction diagram
-
at high concentrations
-
?
ssRNA + H2O
?
show the reaction diagram
-
-
-
-
?
T4 mRNA + H2O
5'-phosphomononucleotides
show the reaction diagram
-
-
-
?
tRNA + H2O
?
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
mRNA + H2O
5'-phosphomononucleotides
show the reaction diagram
precursor tRNA + H2O
mature tRNA + 5'-phosphomononucleotides
show the reaction diagram
RNA
5'-phosphomononucleotides
show the reaction diagram
-
3' to 5'direction only
-
-
?
ss RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Li+
-
can substitute for K+ to a small extend
Mn2+
-
necessary for activity
Na+
-
increases activity against T4 mRNA, can substitute for K+ in activation against T4 mRNA and RNA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
nicotinamide
NAM
trichostatin A
TSA
DNA oligonucleotide with strong duplex structure and 3' single strand
-
-
-
DNA oligonucleotide with strong duplex structure and 5' single strand
-
-
-
DNA oligonucleotide with strong duplex structure, 3' and 5' single strand
-
-
-
DNA oligonucleotide with weak duplex structure and 3' single strand
-
-
-
DNA oligonucleotide with weak duplex structure and 5' single strand
-
-
-
DNA oligonucleotide with weak duplex structure, 3' and 5' single strand
-
-
-
DNA stem-loop structure
-
free 3'- and 5'-arms needed for potent inhibition, weaker stem-loops are better inhibitors than their counterpart with a strong duplex
-
ds plasmid DNA
-
-
-
mixed RNA-DNA oligonucleotides
-
-
-
monovalent or divalent cations
-
Na+
-
substrate: artificial polynucleotides
oligonucleotides
poly(dC)
-
19 to 29 monomer units chain lenght
Poly(U)
-
strong competitive inhibitor of T4 mRNA-degradation
RNA stem-loop structure
-
rRNA
-
weak inhibitor of T4 mRNA-degradation
SDS
-
complete inhibition 10 s after addition of SDS
ss DNA oligonucleotides
-
sucrose
-
slight inhibition, in 1% and 5% sucrose 5% and 20% of the activity inhibited
Urea
-
in 0.5 and 0.05 M urea 58% and 11% of the activity inhibited, complete inhibition at 1 M urea
Zn2+
-
competitive inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cadaverine
-
can replace missing Mg2+ to a small extent
IPTG
-
1 mM, after 2 h RNase major protein in cell extracts of E.coli strain BL21(DE3)
putrescine
-
can replace missing Mg2+ to a small extent
spermidine
-
can replace missing Mg2+ to a small extent
spermine
-
can replace missing Mg2+ to a small extent
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.00125
Poly(A)
0.000075
Poly(U)
-
-
0.0004
polyadenosine
-
pH 7.2, 23°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 80800
Poly(A)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
230 - 236
Poly(A)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
DNA oligonucleotide with strong duplex structure and 3' single strand
-
pH 7.2, 23°C
-
0.0331
DNA oligonucleotide with strong duplex structure and 5' single strand
-
pH 7.2, 23°C
-
0.0014
DNA oligonucleotide with strong duplex structure, 3' and 5' single strand
-
pH 7.2, 23°C
-
0.0008
DNA oligonucleotide with weak duplex structure and 3' single strand
-
pH 7.2, 23°C
-
0.0336
DNA oligonucleotide with weak duplex structure and 5' single strand
-
pH 7.2, 23°C
-
0.0005
DNA oligonucleotide with weak duplex structure, 3' and 5' single strand
-
pH 7.2, 23°C
-
10
EDTA
-
malE-malF mRNA transcripts incubated at 37°C
0.0005 - 0.0148
polydeoxycytidine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
-
activity of the most active fraction, substrate: T4 mRNA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
11% of the optimal activity observed at pH 6.0, 55% at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery. The ability of RNase II to maintain cell viability in the absence of exoribonuclease polynucleotide phosphorylase is markedly diminished when the RNase II cellular structures are lost due to changes in the amphipathicity of the amino-terminal helix
Manually annotated by BRENDA team
RNase II is associated with the cytoplasmic membrane by its amino-terminal amphipathic helix. The helix also acts as an autonomous transplantable membrane binding domain capable of directing normally cytoplasmic proteins to the membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
RNase II is another 3'-5' hydrolytic exoribonuclease from the RNase II family of exoribonucleases
malfunction
metabolism
role for RNase II Lys501 acetylation in modulating cell growth during stress conditions
physiological function
evolution
RNase R is another 3'-5' hydrolytic exoribonuclease from the RNase II family of exoribonucleases
malfunction
metabolism
the enzyme is involved in cell motility and biofilm formation
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
gel filtration
65000
-
sucrose density gradient centrifugation
67000
-
1 * 67000
70000
80000 - 90000
-
native and SDS-PAGE, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
residue Lys501 is acetylated in RNase II. This modification, reversibly controlled by the acetyltransferase Pka and the deacetylase CobB, a SIRT family deacetylase, affects binding of the substrate and thus decreases the catalytic activity of RNase II. Acetylation can regulate the activity of a bacterial ribonuclease. Lys501 is the major site of acetylation in this enzyme, but some other lysine residues in RNase II are also susceptible to acetylation. After enzyme inhibitor nicotinamide treatment, the acetylation level of RNase II increases 2-3fold in both wild-type and mutant strains. Inactivation of CobB increased the acetylation of wild-type RNase II
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native RNase II and its RNA-bound complex
-
three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single stranded RNA
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C284Y
RNase II thermolability of the rnb500 phenotype is due to the Cys284Tyr mutation within the RNB domain, which abolishes activity by increasing protein kinetic instability at the nonpermissive temperature. Expression of RNase II C284Y and the double mutant (D126N and C284Y) does not allow growth at the nonpermissive temperature of 44°C. Structural mapping and partial multiple sequence alignment of RNase II thermosensitive phenotype mutations, overview
D126N
site-directed mutagenesis, the RNase II mutant exhibits a slightly decreased growth at 44°C suggesting some thermosensitivity which does not account for a major phenotype. This individual mutation is not detrimental for the function of RNase II in vivo. the RNase II D126N variant exhibits substantial catalytic activity
D126N/C284Y
site-directed mutagenesis, expression of RNase II C284Y and the double mutant (D126N and C284Y) does not allow growth at the nonpermissive temperature of 44°C
D201N
D201N/E390A
very similar specific specific activity to the wild-type
D201N/Y313F
shows less than 0.1% of the specific activity present in the wild-type
D201N/Y313F/E390A
shows less than 0.1% of the specific activity present in the wild-type
D207N
still retains 12% activity
D210N
significant loss of activity in degradation of poly(A) (0.3% of that of the wild-type enzyme). Generates a 10-11-nt fragment as a major degradation product, although longer reaction times result in the usual 4-nt fragment as a secondary product
E390A
specific activity is very similar to that of the wild-type
E542A
extraordinary catalysis and binding abilities that turns RNase II into a super-enzyme. More than a 100fold increase in the specific exoribonucleolytic activity, significantly increases affinity for the poly(A) substrate
F358A
the protein is 2fold more active than the wild-type
K501Q
site-directed mutagenesis, mutation of Lys501 results in up to 80% reduction in acetylation of RNase II
K501R
site-directed mutagenesis, mutation of Lys501 results in up to 80% reduction in acetylation of RNase II
R500A
shows more than a 40000fold reduction in specific activity when compared with the wild-type
R500K
shows less than 0.1% of the specific activity present in the wild-type
Y253A
26% of the activity of the enzyme persists, significantly impairs RNA binding
Y253A/F358A
12% of the activity of the enzyme persists, whereas RNA binding affinity is not significantly affected
Y313A
100fold reduction of specific activity
Y313F
specific activity is very similar to that of the wild-type
Y313F/E390A
specific activity is not affected
D155M
-
truncated RNase II protein pETIIDELTACSD1DELTAS1 consisting of the nuclease domain alone, but lacking any part of CSD2. Removal of the RNA-binding domains does allow RNase II to proceed further
D201N
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D201N/E390A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D201N/Y313F
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D201N/Y313F/E390A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D207N
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D209N
D210N
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
D278N
-
mutation at the catalytic center of RNase R, is inactive on A(4), but retains 4% activity of wild-type RNase R on poly(A) and A(17)
E390A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
E542A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
F358A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
R500A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
Y253A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
Y253A/F358A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
Y313A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
Y313F
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
Y313F/E390A
-
site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
enzyme inactivation, RNase II is thermolabile
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
RNase R is a highly unstable protein in exponentially growing cells, but is stabilized in stationary phase and other stress conditions. Most of the RNase R in exponential phase has been shown to be linked with ribosomal proteins
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, lyophilized purified enzyme, addition of 25 mg of bovine serum mercaptalbumin, stable for at least 2 months
-
-20°C, small aliquots of purified enzyme, 10% glycerol, stable for at least 19 months
-
-70°C, stable for at least 1 month without loss of activity
-
0°C, half-life of 5-7 days
-
deep frozen, lyophilized crude enzyme, several months, stable
-
frozen, crude enzyme, 1 month, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
all mutants, with the exception of R500K, by histidine affinity chromatography and the AKTA fast protein liquid chromatography system
recombinant His- or FLAG-tagged wild-type non-acetylated and acetylated and mutants from Escherichia coli strain BL21(DE3) by affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
wild-type and RNase II mutants purified by affinity chromatography
by affinity chromatography
-
by centrifugation, ion exchange and hydrophobic interaction chromatography
-
Escherichia coli strain BL21(DE3)
-
partial purification, between 50-100fold
-
RNase R and RNase II constructs, full-length wild-type RNase R and RNase R mutant D278N
-
to apparent homogeneity, 270fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), enzyme expression for complementation in Escherichia coli MG1693-derivative strain CMA401
recombinant overexpression of His-tagged wild-type non-acetylated and acetylated RNase II and of FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) lacking Pka or CobB
vapour-diffusion method, wild-type RNase II is crystallized in two crystal forms, both of which belonged to space group P2(1). X-ray diffraction data are collected to 2.44 and 2.75 A resolution, with unit-cell parameters a = 56.8, b = 125.7, c = 66.2 A, beta = 111.9° and a = 119.6, b = 57.2, c = 121.2 A, beta = 99.7°, respectively. The RNase II D209N mutant gives crystals that belonged to space group P6(5), with unit-cell parameters a = b = 86.3, c = 279.2 A, and diffract to 2.74 A
wild-type and mutants overexpressed from pFCT6.9 vector as His6-tagged fusion proteins in Escherichia coli BL21(DE3)
wild-type and RNase II mutants cloned into plasmid pFCT6.9 and expressed in Escherichia coli BL21(DE3)
X-ray crystallographic structures of both the ligand-free (at 2.44 A resolution) and RNA-bound (at 2.74 A resolution) forms of RNase II. Structures show that RNase II is organized into four domains: two cold-shock domains, one RNB catalytic domain, which has an unprecedented alphabeta-fold, and one S1 domain. The active site is buried within the RNB catalytic domain, in a pocket formed by four conserved sequence motifs. The structure shows that the catalytic pocket is only accessible to single-stranded RNA, and explains the specificity for RNA versus DNA cleavage. It also explains the dynamic mechanism of RNA degradation by providing the structural basis for RNA translocation and enzyme processivity
Escherichia coli strain JM109
-
pACYC184 derivative expressing RNase II, RNase II lacking cold shock domain-1 or mutant D209N under araBAD promoter. PACYC184 derivative expressing RNase R under araBAD promoter. RNase II and mutant D209N overexpressed from pET plasmid constructs in CH12 DELTArna cells
-
RNase II wild-type, mutant and truncated proteins, cloned into plasmid pFCT6.1, overexpressed in Escherichia coli BL21(DE3)
-
RNase R and RNase II constructs cloned into vector pET44R and overexpressed in Escherichia coli BL21II-R-(DE3)pLysS
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activity of RNase R is modulated according to the growth conditions of the cell and is induced under several stress conditions
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
-
RNA-binding domains of RNase II play a more important role in its exoribonuclease activity than they do in the activity of RNase R
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spahr, P.F.
Purification and properties of ribonuclease II from Escherichia coli
J. Biol. Chem.
239
3716-3726
1964
Escherichia coli
Manually annotated by BRENDA team
Nossal, N.G.; Singer, M.F.
The processive degradation of individual polyribonucleotide chains. I. Escherichia coli ribonuclease II
J. Biol. Chem.
243
913-922
1968
Escherichia coli
Manually annotated by BRENDA team
Schmidt, F.J.; McClain, W.H.
An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA
Nucleic Acids Res.
5
4129-4139
1978
Escherichia coli
Manually annotated by BRENDA team
Gupta, R.S.; Kasai, T.; Schlessinger, D.
Purification and some novel properties of Escherichia coli RNase II
J. Biol. Chem.
252
8945-8949
1977
Escherichia coli
Manually annotated by BRENDA team
Cannistraro, V.J.; Kennell, D.
The reaction mechanism of ribonuclease II and its interaction with nucleic acid secondary structures
Biochim. Biophys. Acta
1433
170-187
1999
Escherichia coli
Manually annotated by BRENDA team
Piedade, J.; Zilhao, R.; Arraiano, C.M.
Construction and characterisation of an absolute deletion mutant of Escherichia coli ribonuclease II
FEMS Microbiol. Lett.
127
187-194
1995
Escherichia coli
Manually annotated by BRENDA team
Coburn, G.A.; Mackie, G.A.
Overexpression, purification, and properties of Escherichia coli ribonuclease II
J. Biol. Chem.
271
1048-1053
1996
Escherichia coli
Manually annotated by BRENDA team
Li, Z.; Deutscher, M.P.
The role of individual exoribonucleases in processing at the 3end of Escherichia coli tRNA precursors
J. Biol. Chem.
269
6064-6071
1994
Escherichia coli
Manually annotated by BRENDA team
Guarneros, G.; Portier, C.
Different specificities of ribonuclease II and polynucleotide phosphorylase in 3'-mRNA decay
Biochimie
73
543-549
1991
Escherichia coli
Manually annotated by BRENDA team
Mitchell, P.; Petfalski, E.; Shevchenko, A.; Mann, M.; Tollervey, D.
The exosome: A conserved eukaryotic RNA processing complex containing multiple 3'- to 5'-exoribonucleases
Cell
91
457-466
1997
Escherichia coli
Manually annotated by BRENDA team
Krishna, R.V.; Ko, T.S.; Meyhack, B.; Apirion, D.
On the localization of ribonucleases in bacteria
FEBS Lett.
29
105-108
1973
Escherichia coli
Manually annotated by BRENDA team
Cannistraro, V.J.; Kennell, D.
Escherichia coli ribonuclease II
Methods Enzymol.
342
309-330
2001
Escherichia coli
Manually annotated by BRENDA team
Amblar, M.; Arraiano, C.M.
A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding
FEBS J.
272
363-374
2005
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli SK4803, Escherichia coli JM109
Manually annotated by BRENDA team
Bollenbach, T.J.; Schuster, G.; Stern, D.B.
Cooperation of endo- and exoribonucleases in chloroplast mRNA turnover
Prog. Nucleic Acid Res. Mol. Biol.
78
305-337
2004
Synechocystis sp., Saccharomyces cerevisiae, Caenorhabditis elegans, Chlamydomonas sp., Drosophila sp. (in: flies), Escherichia coli, Haloferax volcanii, Embryophyta, Homo sapiens, Mammalia, no activity in archaebacteria, Streptomyces coelicolor, uncultured Gammaproteobacteria bacterium
Manually annotated by BRENDA team
Amblar, M.; Barbas, A.; Gomez-Puertas, P.; Arraiano, C.M.
The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization
RNA
13
317-327
2007
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
McVey, C.E.; Amblar, M.; Barbas, A.; Cairrao, F.; Coelho, R.; Romao, C.; Arraiano, C.M.; Carrondo, M.A.; Frazao, C.
Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II)
Acta Crystallogr. Sect. F
62
684-687
2006
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Amblar, M.; Barbas, A.; Fialho, A.M.; Arraiano, C.M.
Characterization of the functional domains of Escherichia coli RNase II
J. Mol. Biol.
360
921-933
2006
Escherichia coli
Manually annotated by BRENDA team
Zuo, Y.; Vincent, H.A.; Zhang, J.; Wang, Y.; Deutscher, M.P.; Malhotra, A.
Structural basis for processivity and single-strand specificity of RNase II
Mol. Cell
24
149-156
2006
Escherichia coli
Manually annotated by BRENDA team
Frazao, C.; McVey, C.E.; Amblar, M.; Barbas, A.; Vonrhein, C.; Arraiano, C.M.; Carrondo, M.A.
Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
Nature
443
110-114
2006
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Mohanty, B.K.; Kushner, S.R.
Ribonuclease P processes polycistronic tRNA transcripts in Escherichia coli independent of ribonuclease E
Nucleic Acids Res.
35
7614-7625
2007
Escherichia coli
Manually annotated by BRENDA team
Awano, N.; Inouye, M.; Phadtare, S.
RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase II
J. Bacteriol.
190
5924-5933
2008
Escherichia coli, Escherichia coli JM83
Manually annotated by BRENDA team
Barbas, A.; Matos, R.G.; Amblar, M.; Lpez-Vinas, E.; Gomez-Puertas, P.; Arraiano, C.M.
New insights into the mechanism of RNA degradation by ribonuclease II identification of the residue responsible for setting the RNase II end product
J. Biol. Chem.
283
13070-13076
2008
Homo sapiens, Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Vincent, H.A.; Deutscher, M.P.
The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA
J. Biol. Chem.
284
486-494
2009
Escherichia coli
Manually annotated by BRENDA team
Arraiano, C.M.; Barbas, A.; Amblar, M.
Characterizing ribonucleases in vitro examples of synergies between biochemical and structural analysis
Methods Enzymol.
447
131-160
2008
Escherichia coli, Escherichia coli SK4803
Manually annotated by BRENDA team
Barbas, A.; Matos, R.G.; Amblar, M.; Lopez-Vinas, E.; Gomez-Puertas, P.; Arraiano, C.M.
Determination of key residues for catalysis and RNA cleavage specificity: one mutation turns RNase II into a "SUPER-ENZYME"
J. Biol. Chem.
284
20486-20498
2009
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Garza-Sanchez, F.; Shoji, S.; Fredrick, K.; Hayes, C.S.
RNase II is important for A-site mRNA cleavage during ribosome pausing
Mol. Microbiol.
73
882-897
2009
Escherichia coli
Manually annotated by BRENDA team
Matos, R.G.; Barbas, A.; Arraiano, C.M.
Comparison of EMSA and SPR for the characterization of RNA-RNase II complexes
Protein J.
29
394-397
2010
Escherichia coli
Manually annotated by BRENDA team
Matos, R.G.; Barbas, A.; Gomez-Puertas, P.; Arraiano, C.M.
Swapping the domains of exoribonucleases RNase II and RNase R: conferring upon RNase II the ability to degrade ds RNA
Proteins
79
1853-1867
2011
Escherichia coli
Manually annotated by BRENDA team
Lu, F.; Taghbalout, A.
The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome
Biosci. Rep.
34
e00166
2014
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Lu, F.; Taghbalout, A.
Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II
J. Biol. Chem.
288
7241-7251
2013
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Pobre, V.; Arraiano, C.
Next generation sequencing analysis reveals that the ribonucleases RNase II, RNase R and PNPase affect bacterial motility and biofilm formation in E. coli
BMC Genomics
16
72-83
2015
Escherichia coli (P21499), Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team
Reis, F.P.; Barria, C.; Gomez-Puertas, P.; Gomes, C.M.; Arraiano, C.M.
Identification of temperature-sensitive mutations and characterization of thermolabile RNase II variants
FEBS Lett.
593
352-360
2019
Escherichia coli (P30850), Escherichia coli SK5689 (P30850)
Manually annotated by BRENDA team
Song, L.; Wang, G.; Malhotra, A.; Deutscher, M.P.; Liang, W.
Reversible acetylation on Lys501 regulates the activity of RNase II
Nucleic Acids Res.
44
1979-1988
2016
Escherichia coli (P30850), Escherichia coli
Manually annotated by BRENDA team