Information on EC 3.1.13.1 - exoribonuclease II

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.1.13.1
-
RECOMMENDED NAME
GeneOntology No.
exoribonuclease II
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
BRENDA Link
KEGG Link
MetaCyc Link
tRNA processing
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-24-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Chlamydomonas sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain JM109 and BL21(DE3)
-
-
Manually annotated by BRENDA team
strain JM83
-
-
Manually annotated by BRENDA team
strain SK4803
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain JR32
-
-
Manually annotated by BRENDA team
strain JR32
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
no activity in archaebacteria
except Halobacterium species NRC-1
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
strain SK4803, carrying the mutant allele rnb296, single substitution of aspartate 209 for asparagine
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli SK4803
strain SK4803, carrying the mutant allele rnb296, single substitution of aspartate 209 for asparagine
-
-
Manually annotated by BRENDA team
strain KT2440
UniProt
Manually annotated by BRENDA team
starin BJ5464
-
-
Manually annotated by BRENDA team
strain YJJ
-
-
Manually annotated by BRENDA team
potato
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains T4 and TIGR4
Uniprot
Manually annotated by BRENDA team
strain 427 and 29-13
-
-
Manually annotated by BRENDA team
strain 427 and 29-13
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
instead of A-site cleavage, translational pausing in DELTARNase II cells produces transcripts that are truncated +12 and +28 nucleotides downstream of the A-site codon. Deletion of RNase R has little effect on A-site cleavage. Polynucleotide phosphorylase overexpression restores A-site cleavage activity to DELTARNase II cells
physiological function
additional information
-
stability of RNAse II-RNA interactions and effects on the enzyme reaction mechanism processing and degrading RNA molecules, analysis by surface plasmon resonance and electrophoretic mobility shift Assay, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5' end-labeled pre-tRNASer + H2O
?
show the reaction diagram
degradation of pre-tRNASer in a processive manner, leaving a short oligonucleotide (about 3nt) product
-
-
?
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
duplex RNA + H2O
?
show the reaction diagram
-
-
-
-
?
m-RNA + H2O
?
show the reaction diagram
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
-
-
-
-
?
oligoribonucleotide + H2O
?
show the reaction diagram
petD3 RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
-
-
products detected are exclusively nucleotide monophosphates
-
?
poly (A)
5'-AMP
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
?
show the reaction diagram
-
23 units oligonucleotide
-
-
?
poly[8-3H]adenylic acid + H2O
?
show the reaction diagram
precursor tRNA + H2O
mature tRNA + 5'-phosphomononucleotides
show the reaction diagram
RNA
5'-phosphomononucleotides
show the reaction diagram
RNA
nucleoside 5'-monophosphate
show the reaction diagram
-
-
-
-
?
RNA + H2O
phosphomononucleotides
show the reaction diagram
RNA turnover
-
-
?
rRNA
5'-phosphomononucleotides
show the reaction diagram
rRNA + H2O
?
show the reaction diagram
siRNA + H2O
?
show the reaction diagram
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
?
show the reaction diagram
-
tRNA from Escherichia coli
-
-
?
tRNA + H2O
?
show the reaction diagram
tRNAiMet + H2O
?
show the reaction diagram
complete degradation of the hypomodified tRNA requires both Rrp44 and the poly(A) polymerase activity of TRAMP. The intact exosome lacking only the catalytic activity of Rrp44 fails to degrade tRNAi Met, showing this to be a specific Rrp44 substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
?
RNA
nucleoside 5'-monophosphate
show the reaction diagram
-
-
-
-
?
RNA + H2O
phosphomononucleotides
show the reaction diagram
Q88DE8
RNA turnover
-
-
?
ss RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
tRNAiMet + H2O
?
show the reaction diagram
P39112
complete degradation of the hypomodified tRNA requires both Rrp44 and the poly(A) polymerase activity of TRAMP. The intact exosome lacking only the catalytic activity of Rrp44 fails to degrade tRNAi Met, showing this to be a specific Rrp44 substrate
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
may partly substitute for Mg2+, with less efficiency
KCl
-
preferred concentration is 50 mM. Activity starts to decrease above 150 mM
Li+
-
can substitute for K+ to a small extend
Na+
-
increases activity against T4 mRNA, can substitute for K+ in activation against T4 mRNA and RNA
NaCl
-
enzyme is active in NaCl, but the cleavage efficiency is 10times lower when compared to its activity in KCl
Zn2+
-
induces a folding reaction resulting in protein preparations with 50-60% alpha-helical content and 10-20% beta-sheet structure, critical concentration for refolding bigger or equal to 0.1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-capped mRNA
-
-
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
NaCl
-
a salt concentration of 0.05 M inhibits 50% of the activity, salt optimum: 0.01 M
oligonucleotides
-
competitive inhibition, fragments bind without being destroyed; small to medium sized
p-chloromercuribenzoate
-
-
poly(A) binding protein
-
inhibits degradation of poly(A)+-strands
-
poly(dC)
-
19 to 29 monomer units chain lenght
Poly(U)
-
strong competitive inhibitor of T4 mRNA-degradation
RNA stem-loop structure
-
built by repetitive extragenic palindromic sequences; the lower the stability of the RNA-stem, the faster the degradation
-
RNA with a 2',3'-cyclic phosphate group
-
on the potential substrate molecule
-
RNA with a terminal 3'-phosphate group
Rna with a terminal 5'-phosphate group
-
-
rRNA
-
weak inhibitor of T4 mRNA-degradation
SDS
-
complete inhibition 10 s after addition of SDS
spermine
-
slight inhibition of poly(U)-degradation
ss DNA oligonucleotides
Sucrose
-
slight inhibition, in 1% and 5% sucrose 5% and 20% of the activity inhibited
thymidine nucleotides
-
potent inhibitor, pTp at a concentration of 0.00004 M inhibits degradation of poly(A) by 60%, pTpT at a concentration of 0.0005 M inhibits degradation of poly(A) by 30%
-
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
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, 23C
-
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, 23C
-
0.0331
DNA oligonucleotide with strong duplex structure and 5' single strand
-
pH 7.2, 23C
-
0.0014
DNA oligonucleotide with strong duplex structure, 3' and 5' single strand
-
pH 7.2, 23C
-
0.0008
DNA oligonucleotide with weak duplex structure and 3' single strand
-
pH 7.2, 23C
-
0.0336
DNA oligonucleotide with weak duplex structure and 5' single strand
-
pH 7.2, 23C
-
0.0005
DNA oligonucleotide with weak duplex structure, 3' and 5' single strand
-
pH 7.2, 23C
-
10
EDTA
-
malE-malF mRNA transcripts incubated at 37C
0.05
NaCl
-
salt 0.01 M
0.0005 - 0.0148
polydeoxycytidine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
substrate: poly(A)
0.04
-
activity of the most active fraction, substrate: T4 mRNA
970
-
pH 8.0, 37C
additional information
-
95600 units/mg: one unit is defined as the amount of enzyme producing 0.1 A260 acid-soluble materials in 3 h at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
minor pH optimum
7.5 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
11% of the optimal activity observed at pH 6.0, 55% at pH 9.0
7 - 8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
T-lymphoblastoid
Manually annotated by BRENDA team
-
ERI-1 expression restricted to the speramtheca
Manually annotated by BRENDA team
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
-
DFC region
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
SDS-PAGE
35000
-
gel filtration
37000
-
native state gel filtration
65000
-
sucrose density gradient centrifugation
80000 - 90000
-
native and SDS-PAGE, gel filtration
80000
-
SDS-PAGE
83000
-
gel filtration
88000
-
gel filtration
92000
-
SDS-PAGE
160000
-
SDS-PAGE
175000
-
amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 12967, MALDI-TOF mass spectrometry; x * 13000, SDS-PAGE
monomer
additional information
-
human Rrp44 proteins shows an overall structure similar to that of Escherichia coli 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
-
Rrp44 in complex with single-stranded RNA, to 2.3 A resolution. Structure of Rrp44 displays CSD1, CSD2, RNB, and S1 domains. The two N-terminal cold shock domains (CSD1, residues 271-399; CSD2, residues 400-475) and the C-terminal S1 domain (residues 911-998) display characteristic OB folds, with five antiparallel beta strands organized in a beta barrel structure. CSD1 is fused to an N-terminal alpha helix (residues 261-268) and the S1 domain has an insertion of three beta strands (between beta3 and beta4) as compared to a standard OB fold. The RNB domain is centered around a core and is surrounded by several alpha helices
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
for 5 min, in absence of substrate, less than 1% of activity remains; in presence of substrate, product or deoxy-oligonucleotides (dC)27: active up to 60 min
50
-
in 0.1 M Tris-Cl, pH 8.0, for 15 min, loss of 20-30% of activity; in 0.1 M Tris-Cl, pH 8.0, for 60 min, loss of 40-60% of activity
60
-
for 1 min completely destroys enzyme activity
90
-
for 1 min, no activity remains
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, 1.5 ml aliquots, 1 mg of protein per ml, 6 months, small decrease of activity
-
-20C, lyophilized purified enzyme, addition of 25 mg of bovine serum mercaptalbumin, stable for at least 2 months
-
-20C, small aliquots of purified enzyme, 10% glycerol, stable for at least 19 months
-
-70C, more than 50% of activity after more than a year
-
-70C, stable for at least 1 month without loss of activity
-
0C, half-life of 5-7 days
-
4C, 10-ml fractions containing 1 mg trypsin inhibitor carrier protein because RNase II loses activity under this conditions at protein concentrations below 0.1 mg/ml
-
deep frozen, lyophilized crude enzyme, several months, stable
-
frozen, crude enzyme, 1 month, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
370fold, nearly to homogeneity
-
5300-26500fold, to homogeneity
-
all mutants, with the exception of R500K, by histidine affinity chromatography and the AKTA fast protein liquid chromatography system
-
anion exchange chromatography at denaturing conditions, in some cases followed by isoelectric focusing and dye binding chromatography
-
by affinity chromatography
-
by centrifugation, ion exchange and hydrophobic interaction chromatography
-
by histidine affinity chromatography and an AKTA HPLC system
Escherichia coli strain BL21(DE3)
-
full-length protein and mutants purified by affinity Ni-NTA chromatography, followed by ion exchange chromatography and gel filtration. 242-1001 construct purified to homogeneity
includes glutathione-Sepharose resin chromatography
-
partial purification that includes DEAE-Sepharose chromatography
-
partial purification, 500-700fold
-
partial purification, between 50-100fold
-
purification includes M2-agarose affinity resin
-
purified by inmunoprecipitation
-
purified on protein A-agarose and affinity GST-AtRrp4p inmobilized on nitrocellulose
-
RNase R and RNase II constructs, full-length wild-type RNase R and RNase R mutant D278N
-
Rrp44-exosome (RE) architecture suggests an active site sequestration mechanism for strict control of 3' exoribonuclease activity in the RE complex
-
to apparent homogeneity, 270fold
-
wild-type and RNase II mutants purified by affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA fragments corresponding to the entire open reading frame in each gene are subcloned into a TA cloning vector
-
Escherichia coli strain JM109
-
expressed in Drosophila cell line
-
expressed in Escherichia coli (XL-1)
-
expressed in Escherichia coli as a glutathione-S-transferasa fusion protein
-
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli M15pREP4
-
Expression of rnr mutant (inactivation of Rnase R) is performed in Escherichia coli. Overexpression of genes corresponding to the flagellar apparatus or to the biosynthesis of cofactors by the absence of RNase R gene.
full-length Rrp44 (residues 1-1001) and truncated constructs of Rrp44 expressed from a pETM11 vector in Escherichia coli
into the pET-15b vector, cloned into Escherichia coli DH5alpha, subsequently transformed into Escherichia coli strain BL21(DE3)
-
into the pET-15b vector, transformed into Escherichia coli Novablue, subsequently transformed into Escherichia coli strain BL21(DE3)
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
-
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)
-
wild-type Rrp44, Rrp44-20, and Rrp44-cat are expressed in Escherichia coli as GST fusions
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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/E390A
D201N/Y313F
D201N/Y313F/E390A
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)
R500K
-
shows less than 0.1% of the specific activity present in the wild-type
Y253A/F358A
Y313F/E390A
D209N
-
has less than 1% of the wild-type RNase activity, has similar affinities for the RNA substrate as the wild-type enzyme
-
C425A
-
cannot be classified as polymorphic in the Japanese population. In the Korean, Mongolian, Ovambo, Turkish, and German DNA no genotype other than homozygotic 425C allele in RNASE2 at each single nucleotide polymorphism site is found
D275A
-
is stable and produced in amounts similar to those seen for the wild-type enzyme, but it cannot repress competence
D283R
-
is stable and produced in amounts similar to those seen for the wild-type enzyme, but it cannot repress competence
D275A
-
is stable and produced in amounts similar to those seen for the wild-type enzyme, but it cannot repress competence
-
D283R
-
is stable and produced in amounts similar to those seen for the wild-type enzyme, but it cannot repress competence
-
A815F
degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 4fold) than the wild-type enzyme
A815W
degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 3fold) than the wild-type enzyme
additional information
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
medicine
-
new factor in the IFN-mediated antiviral barrier against HIV-1
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