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Information on EC 3.1.26.4 - ribonuclease H and Organism(s) Escherichia coli and UniProt Accession P10442
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3.1.26.4 ribonuclease HSpecify your search results
Word Map
- 3.1.26.4
-
antiretroviral
- nucleoside
- viruses
-
nnrti
-
virological
-
hiv-infected
-
nonnucleoside
- leukemia
- subtype
-
integrase
- lymphocyte
- strand
- cd4
- efavirenz
-
retroviral
- zidovudine
-
drug-resistant
- infectious
- nevirapine
- retroviruses
- telomerase
- nucleic
- tenofovir
- lamivudine
-
anti-hiv
-
first-line
- virion
- t-cells
-
surveillance
-
retrotransposons
-
haart
- polymerases
-
proviral
-
swab
- covid-19
- coronavirus
- ritonavir
- sars-cov-2
-
outbreak
-
telomeric
-
nucleocapsid
-
rna-dependent
-
resistance-associated
- dntp
-
treatment-naive
-
hiv-positive
-
moloney
- viremia
-
cross-resistance
- pharmacology
- drug development
- analysis
-
once-daily
- molecular biology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
reverse transcriptase, ribonuclease h, rnase h2, rnase hii, rnaseh2a, rnaseh1, ribonuclease hi, ribonuclease h2, rnase hiii, ribonuclease h1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endoribonuclease H
-
-
-
-
hybrid nuclease
-
-
-
-
hybrid ribonuclease
-
-
-
-
hybridase
-
-
-
-
hybridase (ribonuclease H)
-
-
-
-
nuclease, hybrid ribo-
-
-
-
-
nuclease, ribo-, H
-
-
-
-
P32
-
-
-
-
ribonuclease H
ribonuclease HI
RNA*DNA hybrid ribonucleotidohydrolase
-
-
-
-
RNase H
RNase H1
RNase HI
RNase HII
RNase HIII
-
-
-
-
ribonuclease H
-
-
-
-
RNase H
-
-
-
-
RNase H
-
-
RNase H1
-
-
-
-
RNase HI
-
-
-
-
RNase HII
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to a 5'-phosphomonoester
Asp10 is critical for activity and involved in binding of divalent metal ion
-
Endonucleolytic cleavage to a 5'-phosphomonoester
Asp10, Glu48, Asp70, and Asp134 are involved in catalysis, role of Mn2+ in catalysis, mechanism
Endonucleolytic cleavage to a 5'-phosphomonoester
active site residues D10, E48, D70, and D134 are involved in metal ion binding, overview
-
Endonucleolytic cleavage to a 5'-phosphomonoester
evolutionary conserved flexible regions are important for catalysis, structure function relationship, enthalpic/entropic compensation mechanism, overview
-
Endonucleolytic cleavage to a 5'-phosphomonoester
possible mechanisms for the RNase HII-catalysed reaction consistent with the pH-dependent behaviour of the enzyme, the active sites of RNase H enzymes contain a cluster of four strictly conserved carboxylate groups, requirement for ionisation of an active site carboxylic acid for metal ion binding or correct positioning of metal ion in the enzyme-substrate complex and a role for a second active site carboxylate in general base catalysis
-
Endonucleolytic cleavage to a 5'-phosphomonoester
mechanism of RNase H mediated cleavage of the RNA, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9050-76-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1S,3R,4R,5R,7S)-1-[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
(1S,3R,4R,5R,7S)-3-[4-(benzylamino)-5-methyl-2-oxopyrimidin-1(2H)-yl]-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
(1S,3R,4R,5S,7S)-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
(1S,3R,4R,5S,7S)-3-(2-acetamido-6-oxo-5,6-dihydro-9H-purin-9-yl)-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
(1S,3R,4R,5S,7S)-3-[4-(benzylamino)-5-methyl-2-oxopyrimidin-1(2H)-yl]-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
(1S,3R,4R,5S,7S)-3-[6-(benzylamino)-9H-purin-9-yl]-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-7-ol + H2O
?
-
-
-
-
?
(1S,3R,4R,5S,7S)-3-[6-(benzylamino)-9H-purin-9-yl]-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-7-yl 2-cyanoethyl N,N-dipropan-2-ylphosphoramidoite + H2O
?
-
-
-
-
?
1-[(1R,5S,7R,8S)-8-(benzyloxy)-5-[(benzyloxy)methyl]-6-oxabicyclo[3.2.1]octan-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione + H2O
?
-
-
-
-
?
1-[(1S,3R,4R,5R,7S)-7-(benzyloxy)-1-[(benzyloxy)methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidine-2,4(1H,3H)-dione + H2O
?
-
-
-
-
?
1-[(1S,3R,4R,5R,7S)-7-[bis(4-methoxyphenyl)(phenyl)methoxy]-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidine-2,4(1H,3H)-dione + H2O
?
-
-
-
-
?
1-[(1S,3R,4R,5S,7S)-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-7-hydroxy-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidine-2,4(1H,3H)-dione + H2O
?
-
-
-
-
?
1-[(1S,3R,4R,5S,7S)-7-(benzyloxy)-1-[(benzyloxy)methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidine-2,4(1H,3H)-dione + H2O
?
-
-
-
-
?
4-(benzylamino)-1-[(1S,3R,4R,5R,7S)-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-7-hydroxy-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidin-2(1H)-one + H2O
?
-
-
-
-
?
4-(benzylamino)-1-[(1S,3R,4R,5S,7S)-1-[[bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-7-hydroxy-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-5-methylpyrimidin-2(1H)-one + H2O
?
-
-
-
-
?
DNA-(1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid + H2O
?
-
-
-
-
?
DNA-(2'-alkoxy-1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
dsDNA oligonucleotide with a single ribose + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
-
preferred substrate, enzyme excises misincorporated ribonucleotides in DNA
-
-
?
N-(9-[(1S,3R,4R,5S,7S)-7-(benzyloxy)-1-[(benzyloxy)methyl]-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-6-oxo-6,9-dihydro-5H-purin-2-yl)acetamide + H2O
?
-
-
-
-
?
N-benzyl-9-[(1S,3R,4R,5S,7S)-1-([bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-5-methyl-7-[(trimethylsilyl)oxy]-2-oxabicyclo[2.2.1]heptan-3-yl)-9H-purin-6-amine + H2O
?
-
-
-
-
?
N-[9-[(1S,3R,4R,5S,7S)-1-([bis(4-methoxyphenyl)(phenyl)methoxy]methyl]-7-hydroxy-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-6-oxo-6,9-dihydro-5H-purin-2-yl)acetamide + H2O
?
-
-
-
-
?
N-[9-[(1S,3R,4R,5S,7S)-7-hydroxy-1-(hydroxymethyl)-5-methyl-2-oxabicyclo[2.2.1]heptan-3-yl]-6-oxo-6,9-dihydro-5H-purin-2-yl]acetamide + H2O
?
-
-
-
-
?
PPT-RNA + H2O
?
-
single-stranded, the DNA-linked enzyme mutant shows highly reduced activity compared to the wild-type enzyme, specific cleavage of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA
-
-
?
RNA*2'F-ANA-DNA hybrid + H2O
?
-
cleaves the RNA portion of hybrid duplexes of butyl-modified 2'F-ANA-DNA oligonucleotides containing acyclic interresidue units with complementary RNA
-
-
?
RNA*antisense-DNA hybrid + H2O
?
-
cleaves the RNA portion of hybrid duplexes of modified antisense DNA oligonucleotides containing acyclic interresidue units with complementary RNA
-
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme could be involved in the removal of RNA primers during DNA replication
-
-
?
[(1S,3R,4R,5S,7S)-3-[6-(benzylamino)-9H-purin-9-yl]-5-methyl-7-[(trimethylsilyl)oxy]-2-oxabicyclo[2.2.1]heptan-1-yl]methanol + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase HII specifically catalyses the hydrolysis of phosphate diester linkages contained within the RNA portion of DNA/RNA hybrids, usage of 5'-fluorescent oligodeoxynucleotide substrates
-
-
?
DNA-RNA hybrid + H2O
DNA + 5'-phosphonucleotides
-
RNase H binds RNA-DNA hybrid and double-stranded RNA duplexes with similar affinity, but only cleaves the RNA in the former in a specific manner, substrate recognition, overview
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
preference for RNA-DNA hybrid but low activity towards ss and ds RNA and DNA
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
most active substrate: (rA)n-(dT)n
-
?
RNA*DNA hybrid + H2O
?
12 bp and 29 bp oligomers, cleavage site specificity depends on bound metal ion, wild-type end mutant enzymes
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
oligoribonucleotides with 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
hybrid between viral f1 and its complementary RNA, slight preference for cleavage adjacent to pyrimidine
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
phiX174DNA-RNA
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
digestion of more than 95% of the RNA in RNA-DNA hybrids to acid-soluble products
oligoribonucleotides with 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
degrades only an RNA chain hydrogen bonded to DNA
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
oligoribonucleotides with 3'-hydroxyl and 5'-phosphate termini
?
additional information
?
-
substrate cleavage mode of the enzyme, cleavage site specificity
-
-
?
additional information
?
-
-
substrate cleavage mode of the enzyme, cleavage site specificity
-
-
?
additional information
?
-
-
the enzyme cannot cleave the phosphodiester bond covalently linking ribonucleotides to DNA
-
-
?
additional information
?
-
-
substrate characterizationa and substrate specificity
-
-
?
additional information
?
-
-
determination of RNase H cleavage potential of the RNA strand basepaired with the complementary antisense oligonucleotides containing North-East conformationally constrained 1',2'-methylene-bridged azetidine-T and oxetane-T nucleosides, North-constrained 2',4'-ethylene-bridged aza-ENA-T nucleoside, and 2'-alkoxy modified nucleosides, i.e. 2'-O-Me-T and 2'-O-MOE-T modifications, molecular dynamics, overview
-
-
?
additional information
?
-
-
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids
-
-
?
additional information
?
-
ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function
-
-
?
additional information
?
-
-
ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function
-
-
?
additional information
?
-
cleavage of R9-D9*/D18, R2-D9*/D18, R1-D9*/D18, *D8-R1-D9/D18, D8-R1-D9*/D18, and *D18/D18 duplexes substrates by Escherichia coli RNase H1. Escherichia coli RNase H1 cleaves an Okazaki fragment-like substrate most effectively at R(-2)-R(-1) and less effectively at the RNA-DNA junction in the presence of 5 mM MnCl2, indicating that the RNase H1 exhibits a weak 3'-JRNase activity for this substrate in the presence of manganese ions
-
-
?
additional information
?
-
-
cleavage of R9-D9*/D18, R2-D9*/D18, R1-D9*/D18, *D8-R1-D9/D18, D8-R1-D9*/D18, and *D18/D18 duplexes substrates by Escherichia coli RNase H1. Escherichia coli RNase H1 cleaves an Okazaki fragment-like substrate most effectively at R(-2)-R(-1) and less effectively at the RNA-DNA junction in the presence of 5 mM MnCl2, indicating that the RNase H1 exhibits a weak 3'-JRNase activity for this substrate in the presence of manganese ions
-
-
?
additional information
?
-
-
substitution of a single native nucleotide in the antisense strand (AON) by locked nucleic acid (LNA) or by diastereomerically pure carba-LNA results in site-dependent modulation of RNase H1 promoted cleavage of complementary mRNA strands by 2 to 5 fold at 5'-GpN-3' cleavage sites, giving up to 70% of the RNA cleavage products. The 2nd best cleavage site, being the 5'-ApN-3' sites, cleaves up to 23%, depending upon the substitution site in 36 isosequential complementary AONs. A comparison of the modified AON promoted RNA cleavage rates with that of the native AON shows that sequence-specificity is considerably enhanced as a result of modification. Clearly, relatively weaker 5'-purine (Pu)-pyrimidine (Py)-3' stacking in the complementary RNA strand is preferred (giving about 90% of total cleavage products), which plays an important role in RNase H promoted RNA cleavage. A plausible mechanism of RNase H mediated cleavage of the RNA has been proposed to be 2fold, dictated by the balancing effect of the aromatic character of the purine aglycone: first, the locally formed 9-guanylate ion alters the adjoining sugar-phosphate backbone around the scissile phosphate, transforming its sugar N/S conformational equilibrium, to preferential S-type, causing preferential cleavage at 5'-GpN-3' sites around the center of 20 mer complementary mRNA. Second, the weaker nearest-neighbor strength of 5'-Pu-p-Py-3' stacking promotes preferential 5'-GpN-3' and 5'-ApN-3' cleavage, providing about 90% of the total products, compared to about 50% in that of the native one, because of the cLNA/LNA substituent effect on the neighboring 5'-Pu-p-Py-3' sites, providing both local steric flexibility and additional hydration. This facilitates both the water and water/Mg2+ ion availability at the cleavage site causing sequence-specific hydrolysis of the phosphodiester bond of scissile phosphate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme could be involved in the removal of RNA primers during DNA replication
-
-
?
additional information
?
-
-
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids
-
-
?
additional information
?
-
ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function
-
-
?
additional information
?
-
-
ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
Mg2+
Mn2+
additional information
Mg2+
-
binding involves Asp10 and is pH-dependent, binds in the active site pocket of the natively folded enzyme only, stabilizes the enzyme conformation, effect of metal binding on enzyme folding kinetics
Mg2+
maximal activity at 5 mM, binds to metal ion binding site 1 not 2, required, can substitute for Mn2+
Mn2+
required, maximal activity at 0.002-0.005 mM, can substitute for Mg2+, activates up to 0.1 mM, inhibitory above, enzyme contains 2 metal ion binding sites 1 and 2 with regulatory influence on each other, activating metal ion binding site is site 1, inhibitory binding site is site 2, overview, mutants E48A, E48Q, D134A, and D134N have only 1 active Mn2+-binding site
Mn2+
-
activates, two single binding sites: site 1 is formed by Glu48, Asp10, and Asp70, site 2 is formed by Asp10 and Asp134, Glu48 and Asp134 are absolutely required for enzyme activation, binding structure and one-to-two metal mechanism, overview
additional information
no activation by Ca2+, Zn2+, Ba2+, Ni2+, Cu2+, Fe2+, and Sr2+
additional information
-
no activation by Ca2+, Zn2+, Ba2+, Ni2+, Cu2+, Fe2+, and Sr2+
additional information
metal ion binding sites are located in the active site
additional information
-
metal ion binding sites are located in the active site
additional information
-
no activity in absence of Mg2+ or Mn2+, and in presence of 10 mM of Ba2+, Ca2+, Co2+, Zn2+, Cu2+, Fe2+, or Sr2+
additional information
RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-thujaplicin
-
i.e. 2-hydroxy-3-(1-methylethyl)-2,4,6-cycloheptatrien-1-one, slight inhibition
beta-thujaplicin
-
i.e. 2-hydroxy-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one, slight inhibition
beta-thujaplicinol
-
i.e. 2,7-dihydroxy-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
gamma-thujaplicin
-
i.e. 2-hydroxy-5-(1-methylethyl)-2,4,6-cycloheptatrien-1-one, slight inhibition
manicol
-
i.e. 1,2,3,4-tetrahydro-2,7-dihydroxy-9-methyl-2-(1-methylethyl)-6H-benzocyclohepten-6-one
Mn2+
wild-type enzyme, above 0.1 mM, activating below, activating metal ion binding site is site 1, inhibitory binding site is site 2
nootkatin
-
i.e. 2-hydroxy-5-(3-methyl-2-butenyl)-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one, slight inhibition
additional information
-
selectivity of tropolone derivatives for RNase H, IC50 values, inhibition mechanism, overview
-
Ca2+
calcium ions generally inactivate the enzyme and abolish catalysis
Dextran
-
inhibits degradation of poly(rA)*poly(dT), no inhibition of degradation by phi174DNA-RNA. Dextran does not interfere with the recognition site, but rather blocks hydrolysis
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000122
DNA-(1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid
-
pH 7.5, 21°C
-
0.000242
DNA-(2'-alkoxy-1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid
-
pH 7.5, 21°C
-
0.00026
RNA*DNA hybrid
-
pH 8.5, 30°C, recombinant soluble non-tagged enzyme
-
additional information
additional information
-
folding kinetics of the enzyme with Mg2+ bound or metal-free
-
additional information
additional information
-
determination of enzyme surface enzyme kinetics by surface plasmon resonance imaging and surface plasmon fluorescence spectroscopy, kinetic analysis, overview
-
additional information
additional information
-
thermodynamics, heat capacity measurement, thermal stability and flexibility of the enzyme
-
additional information
additional information
-
binding affinity of the chimeric antisense oligonucleotides to the target RNA and DNA, Michaelis-Menten kinetics, overview, dependence of the initial velocity on the substrate concentration, overview
-
additional information
additional information
-
Michaelis-Menten kinetics with different DNA-RNA hybrids
-
additional information
additional information
-
detailed kinetic study of 36 single modified AON-RNA heteroduplexes with the enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.43
DNA-(1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid
-
pH 7.5, 21°C
-
2.5
DNA-(2'-alkoxy-1',2'-methylene-bridged azetidine-T)-antisense-RNA hybrid
-
pH 7.5, 21°C
-
additional information
additional information
-
the logarithm of the turnover number of the enzyme increases steeply with pH until a pH-independent region is reached close to neutrality
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity of wild-type and mutant enzymes, determination by spectrophotometric assay, at different temperatures
additional information
-
the activity of the recombinant soluble enzyme is slightly higher than that of the recombinant refolded enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
the logarithm of the turnover number of the enzyme increases steeply with pH until a pH-independent region is reached close to neutrality, the pH-dependence of log 1/KM is a sigmoidal curve reaching a maximal value at higher pH, suggesting deprotonation of a residue stabilises substrate binding
additional information
-
folding/unfolding and metal binding at different pH values
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.8
-
enzyme is inactive below pH 7.0, activity increases with increasing pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses
malfunction
disruption of the rnhA gene has been reported to increase a basal level of SOS expression in Escherichia coli, probably due to persistence of R-loops on the chromosome
physiological function
additional information
physiological function
ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function. Escherichia coli RNase H1 exhibits 3'-JRNase activity for dsDNAR1 much more effectively in the presence of manganese ions than in the presence of magnesium ions, regardless of whether this substrate is cleaved by 5'-JRNase activity of Escherichia coli RNase H2 in advance or not, and can excise the single ribonucleotide in collaboration with Escherichia coli RNase H2. Not only RNase H2 but also RNase H1 is involved in the RER pathway. Role of RNase H1 in DNA repair: removal of single ribonucleotide misincorporated into DNA in collaboration with RNase H2. The 3'-JRNase activity of Escherichia coli RNase H1 may not be involved in SOS response, because this activity may not be required for R-loop resolution
physiological function
the RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life
additional information
three-dimensional structure is solved, revealing a conserved protein architecture, the RNase H fold
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
additional information
additional information
-
identification and analysis of folding core and flexible regions, which are evolutionary conserved important for catalysis, conserved quantitative stability/flexibility relationships, QSFR, overview
additional information
-
the enzyme shows a mixed beta-sheet with asymmetric alpha helices, and contains the C-helix, or basic loop, structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4-10 mg/ml purifed recombinant wild-type and mutant D10A enzymes, in 20 mM HEPES, pH 7.0-8.0, 5-15% PEG 3350, hanging drop vapour diffusion method and microseeding, several weeks, X-ray diffraction structure determination and analysis
-
purified recombinant enzyme mutants with Mn2+ bound at the active sites, sitting drop vapour diffusion method, 6.7-9.9 mg/ml protein in 20 mM HEPES-NaOH, pH 7.0, 5-10 mm MnCl2, 20-28% PEG 3350, and 10% glycerol, 3 weeks, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution
-
RNase HI-dsRNA enzyme-inhibitor complexes with 9-mer and 10-mer RNA, sitting-drop vapor-diffusion method, 0.001-0.002 ml of 0.11-0.15 mM protein solution is mixed with an equal volume of reservoir solution containing 50 mM bis-Tris, pH 6.1, 12.5% PEG 3350, 25 mM NaCl, 2 mM MgCl2 and 1 mM TCEP, addition of 20 mM HEPES pH 8.0, 16% PEG 3350, molecular replacement, X-ray diffraction structure determination and anaylsis at 3.5-4.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C13A/C63A/C133A/E135C
-
site-directed mutagenesis, 37% activity compared to the wild-type enzyme
D10A
D10A/I53D
-
mutations simultaneously destabilize the core and stabilize the periphery of the protein. Comparison with stabilized mutant D10A, reference protein for two-state folding
D10N
site-directed mutagenesis, active site mutant, 1700fold increased dissociation constants for binding of Mn2+ compared to the wild-type enzyme
D134A
site-directed mutagenesis, mutant shows activity in presence of Mn2+, activity is similar to the wild-type enzyme, but the mutant is not inhibited by Mn2+ concentrations above 0.1 mM in contrast to the wild-type enzyme, 5.0fold increased dissociation constants for binding of Mn2+
D134A/L87A
-
site-directed mutagenesis, crystal structure analysis with bound Mn2+
D134N
site-directed mutagenesis, mutant shows high activity in presence of Mn2+ without inhibition at higher Mn2+ concentrations, and 5.4fold increased dissociation constants for binding of Mn2+
D70N
site-directed mutagenesis, active site mutant, 440fold increased dissociation constants for binding of Mn2+ compared to the wild-type enzyme
E48A
site-directed mutagenesis, mutant shows activity in presence of Mn2+, activity is similar to the wild-type enzyme, but the mutant is not inhibited by Mn2+ concentrations above 0.1 mM in contrast to the wild-type enzyme, 10fold increased dissociation constants for binding of Mn2+
E48A/D134A
site-directed mutagenesis, active site mutant, highly reduced activity and 65fold increased dissociation constants for binding of Mn2+ compared to the wild-type enzyme
E48A/D134N
site-directed mutagenesis, active site mutant, reduced activity and 260fold increased dissociation constants for binding of Mn2+ compared to the wild-type enzyme
E48A/L87A
-
site-directed mutagenesis, crystal structure analysis with bound Mn2+
E48A/L87A/D134A
-
site-directed mutagenesis, crystal structure analysis with bound Mn2+
E48Q
site-directed mutagenesis, mutant shows activity in presence of Mn2+ and 9.2fold increased dissociation constants for binding of Mn2+ compared to the wild-type enzyme
I25A
large destabilization, compared to wild-type. Mutant is active and retains a native-like fold. Mutation results in the equilibrium population of the folding intermediate under near-native conditions. The intermediate is undetectable in a series of heteronuclear single quantum coherences, revealing the dynamic nature of this partially unfolded form on the timescale of NMR detection
additional information
D10A
-
site-directed mutagenesis, active site mutant, no metal binding, altered folding kinetics in absence of metal ions to the values for wild-type enzyme in presence of metal ions
D10A
site-directed mutagenesis, active site mutant, poor binding of Mn2+
D10A
-
mutation relieves charge repulsion in the periphery of the protein and stabilizes the protein by more than 3 kcal/mol. Comparison with mutant D10A/I53D, reference protein for three-state folding
additional information
-
a Cys residue is substituted for Glu135 by site-directed mutagenesis in the mutant enzyme, in which all 3 free Cys residues are replaced by Ala and coupled with a maleimide group which is attached to the 5'-terminus of the nonadeoxyribonucleotide, 5'-GTCATCTCC-3', with a flexible tether. The resulting hybrid enzyme d9-C135/RNase H cleaves the phosphodiester bond between the fifth and sixth residues of the complementary nonaribonucleotide without addition of the oligodeoxyribonucleotide. The nonaribonucleotide is cleaved by the wild-type or unmodified mutant enzyme only when the complemetary oligoribonucleotide is present
additional information
-
a Cys residue is substituted for Glu135 by site-directed mutagenesis in the mutant enzyme, in which all 3 free Cys residues are replaced by Ala and coupled with a maleimide group which is attached to the 5'-terminus of the nonadeoxyribonucleotide, 5'-GTCATCTCC-3', with a flexible tether. The resulting hybrid enzyme d9-C135/RNase H shows site-specific cleavage of the 22-base RNA, 132-base RNA and 534-base RNA which contain a single target sequence, primarily at the unique phosphodiester bond within the target sequence. The hybrid enzyme performs multiple turnovers and at a substrate/enzyme ratio of 10:1 the RNAs are almost completely cleaved
additional information
-
all 3 Cys replaced with Ala, The recombinant enzyme is active and folds reversibly
additional information
-
construction of DNA-linked mutant enzyme, by cross-linking of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA, i.e. PPT-RNA, to the thiol group of Cys135 of the enzyme, mutant shows 4.2% activity compared to the wild-type enzyme
additional information
-
deletion of the basic loop in Escherichia coli RNase H inhibits but does not abolish activity. If the basic loop in Escherichia coli RNase H is inserted into an isolated inactive HIV-1 RNase H domain, Mn2+-dependent activity is partially restored
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
additional information
-
melting temperature is 66°C, conserved quantitative stability/flexibility relationships, QSFR, thermodynamics, thermal stability and flexibility of the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
metal binding stabilizes the enzyme by decreasing its unfolding rate, mechanism
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.025 mg enzyme per ml, in 0.1 M Tris-HCl, pH 7.5, 0.01 MgCl2, 20 mM urea, 1 mM DTT, 0.1% Triton X-100, 50% v/v glycerol, stable for several weeks
-
-20°C, 25 mM Tris-HCl, pH 7.5, 30 mM NaCl, 0.5 mM EDTA, 5 mM 2-mercaptoethanol, 50% glycerol, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, DEAE-cellulose column chromatography, phosphocellulose P11 column chromatography, and heparin Sepharose column chromatography
-
recombinant insoluble enzyme in a urea-denatured form, recombinant soluble intein-tagged enzyme
-
recombinant mutant enzymes from strain HB101 by heparin affinity chromatography
-
recombinant RNase H1 from Escherichia coli strain MIC3009 to homogeneity
recombinant RNase HII from strain BL21(DE3) to near homogeneity by a combination of ion exchange and affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rnhA, recombinant overexpression of RNase H1 in Escherichia coli strain MIC3009
gene rnhB, overexpression of the enzyme in an insoluble form in different strains of Escherichia coli, overexpression of soluble enzyme with a self-cleavable intein-tag
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
comparison of the folding trajectories of the three-state RNase H mutant D10A and the two-state RNase H mutant D10A/I53D, proteins with the same native-state topology but altered regional stability. Both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants
-
study on thermal and mechanical folding and unfolding mechanisms. Mechanical and thermal unfolding proceed through three stable states that are similar. The one difference between the two regimes is in the transition occurring at the most denaturing conditions. For the thermal case, both secondary and tertiary structures melt. For the mechanical case, the secondary structure of the helices remains largely intact, while the bundle itself unfolds. Of the major secondary structure motifs, alpha-helices are more stable than beta-sheets
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
hybrid RNase H molecules with various oligodeoxyribonucleotides may facilitate structural studies of RNA and prove useful as tool for RNA manipulations
analysis
-
facile method that identifies single-stranded regions in RNA using short, randomized DNA oligonucleotides and RNase H cleavage. These regions are then used as constraints in secondary structure prediction. This method was used to improve the secondary structure prediction of Escherichia coli 5S rRNA. The addition of constraints from RNase H cleavage improves the prediction to 100% of base pairs. The same method was used to generate secondary structure constraints for yeast tRNAPhe, which is accurately predicted in the absence of constraints to 95%. The method is advantageous over other single-stranded nucleases since RNase H is functional in physiological conditions and can be used for any RNA to identify accessible binding sites for oligonucleotides or small molecules
analysis
-
quadruplex-based fluorescence assay for sensitive, facile, real-time, and label-free detection of RNase H activity and inhibition by using a G-quadruplex formation strategy. A RNA-DNA substrate is prepared, with the DNA strand designed as a quadruplex-forming oligomer. Upon cleavage of the RNA strand by RNase H, the released G-rich DNA strand folds into a quadruplex in the presence of monovalent ions and interacts with a specific G-quadruplex binder, N-methyl mesoporphyrin IX, giving a dramatic increase in fluorescence and serving as a reporter of the reaction. The assay is simple in design, fast in operation and convenient
REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crouch, R.J.; Dirksen, M.L.
Ribonuclease H
Cold Spring Harbor Monogr. Ser.
14
211-254
1982
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus laevis
-
Itaya, M.
Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene
Proc. Natl. Acad. Sci. USA
87
8587-8591
1990
Escherichia coli
Henry, C.M.; Ferdinand, F.J.; Knippers, R.
A hybridase from Escherichia coli
Biochem. Biophys. Res. Commun.
50
603-611
1973
Escherichia coli
Miller, H.I.; Riggs, A.D.; Gill, G.N.
Ribonuclease H (hybrid) in Escherichia coli. Identification and characterization
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248
2621-2624
1973
Escherichia coli
Berkower, I.; Leis, J.; Hurwitz, J.
Isolation and characterization of an endonuclease from Escherichia coli specific for ribonucleic acid in ribonucleic acid-deoxyribonucleic acid hybrid structures
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248
5914-5921
1973
Escherichia coli
Kanaya, S.; Kohara, A.; Miyagawa, M.; Matsuzaki, T.; Morikawa, K.; Ikehara, M.
Overproduction and preliminary crystallographic study of ribonuclease H from Escherichia coli
J. Biol. Chem.
264
11546-11549
1989
Escherichia coli
Dirksen, M.L.; Crouch, R.J.
Selective inhibition of RNase H by dextran
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256
11569-11573
1981
Escherichia coli
Kanaya, S.; Nakai, C.; Konishi, A.; Inoue, H.; Ohtsuka, E.; Ikehara, M.
A hybrid ribonuclease H. A novel RNA cleaving enzyme with sequence-specific recognition
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267
8492-8498
1992
Escherichia coli
Yang, W.; Hendrickson, W.A.; Kalman, E.T.; Crouch, R.J.
Expression, purification, and crystallization of natural and selenomethionyl recombinant ribonuclease H from Escherichia coli
J. Biol. Chem.
265
13553-13559
1990
Escherichia coli
Nakai, C.; Konishi, A.; Komatsu, Y.; Inoue, H.; Ohtsuka, E.M.; Kanaya, S.
Sequence-specific cleavage of RNA by hybrid ribonuclease H
FEBS Lett.
339
67-72
1994
Escherichia coli
Kanaya, S.; Itaya, M.
Expression, purification, and characterization of a recombinant ribonuclease H from Thermus thermophilus HB8
J. Biol. Chem.
267
10184-10192
1992
Escherichia coli, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Huang, H.W.; Cowan, J.A.
Metallobiochemistry of the magnesium ion. Characterization of the essential metal-binding site in Escherichia coli ribonuclease H
Eur. J. Biochem.
219
253-260
1994
Escherichia coli
Dabora, J.M.; Marqusee, S.
Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state
Protein Sci.
3
1401-1408
1994
Escherichia coli
Tsunaka, Y.; Haruki, M.; Morikawa, M.; Oobatake, M.; Kanaya, S.
Dispensability of glutamic acid 48 and aspartic acid 134 for Mn2+-dependent activity of Escherichia coli ribonuclease HI
Biochemistry
42
3366-3374
2003
Escherichia coli (P0A7Y4), Escherichia coli
Mangos, M.M.; Min, K.L.; Viazovkina, E.; Galarneau, A.; Elzagheid, M.I.; Parniak, M.A.; Damha, M.J.
Efficient RNase H-directed cleavage of RNA promoted by antisense DNA or 2'F-ANA constructs containing acyclic nucleotide inserts
J. Am. Chem. Soc.
125
654-661
2003
Escherichia coli, Homo sapiens
Ohtani, N.; Haruki, M.; Muroya, A.; Morikawa, M.; Kanaya, S.
Characterization of ribonuclease HII from Escherichia coli overproduced in a soluble form
J. Biochem.
127
895-899
2000
Escherichia coli
Rydberg, B.; Game, J.
Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts
Proc. Natl. Acad. Sci. USA
99
16654-16659
2002
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Pyrococcus furiosus
Haruki, M.; Nogawa, T.; Hirano, N.; Chon, H.; Tsunaka, Y.; Morikawa, M.; Kanaya, S.
Efficient cleavage of RNA at high temperatures by a thermostable DNA-linked ribonuclease H
Protein Eng.
13
881-886
2000
Escherichia coli, Thermus thermophilus
Goedken, E.R.; Keck, J.L.; Berger, J.M.; Marqusee, S.
Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI
Protein Sci.
9
1914-1921
2000
Escherichia coli
Fang, S.; Lee, H.J.; Wark, A.W.; Kim, H.M.; Corn, R.M.
Determination of ribonuclease H surface enzyme kinetics by surface plasmon resonance imaging and surface plasmon fluorescence spectroscopy
Anal. Chem.
77
6528-6534
2005
Escherichia coli
Chon, H.; Tadokoro, T.; Ohtani, N.; Koga, Y.; Takano, K.; Kanaya, S.
Identification of RNase HII from psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H
FEBS J.
273
2264-2275
2006
Escherichia coli (P10442), Escherichia coli, Shewanella sp. (Q25C12), Shewanella sp. SIB1 (Q25C12)
Tsunaka, Y.; Takano, K.; Matsumura, H.; Yamagata, Y.; Kanaya, S.
Identification of single Mn2+ binding sites required for activation of the mutant proteins of E. coli RNase HI at Glu48 and/or Asp134 by X-ray crystallography
J. Mol. Biol.
345
1171-1183
2005
Escherichia coli
Budihas, S.R.; Gorshkova, I.; Gaidamakov, S.; Wamiru, A.; Bona, M.K.; Parniak, M.A.; Crouch, R.J.; McMahon, J.B.; Beutler, J.A.; Le Grice, S.F.J.
Selective inhibition of HIV-1 reverse transcriptase-associated ribonuclease H activity by hydroxylated tropolones
Nucleic Acids Res.
33
1249-1256
2005
Escherichia coli, Homo sapiens
Livesay, D.R.; Jacobs, D.J.
Conserved quantitative stability/flexibility relationships (QSFR) in an orthologous RNase H pair
Proteins
62
130-143
2006
Escherichia coli, Thermus thermophilus
Loukachevitch, L.V.; Egli, M.
Crystallization and preliminary X-ray analysis of Escherichia coli RNase HI-dsRNA complexes
Acta Crystallogr. Sect. F
63
84-88
2007
Escherichia coli
Honcharenko, D.; Barman, J.; Varghese, O.P.; Chattopadhyaya, J.
Comparison of the RNase H cleavage kinetics and blood serum stability of the north-conformationally constrained and 2-alkoxy modified oligonucleotides
Biochemistry
46
5635-5646
2007
Escherichia coli
Bastock, J.A.; Webb, M.; Grasby, J.A.
The pH-dependence of the Escherichia coli RNase HII-catalysed reaction suggests that an active site carboxylate group participates directly in catalysis
J. Mol. Biol.
368
421-433
2007
Escherichia coli
Moriguchi, T.; Sakai, H.; Suzuki, H.; Shinozuka, K.
Spermine moiety attached to the C-5 position of deoxyuridine enhances the duplex stability of the phosphorothioate DNA/complementary DNA and shows the susceptibility of the substrate to RNase H
Chem. Pharm. Bull.
56
1259-1263
2008
Escherichia coli
Hu, D.; Pu, F.; Huang, Z.; Ren, J.; Qu, X.
A quadruplex-based, label-free, and real-time fluorescence assay for RNase H activity and inhibition
Chemistry
16
2605-2610
2010
Escherichia coli
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Thermal and mechanical multistate folding of ribonuclease H
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131
235101
2009
Escherichia coli
Connell, K.B.; Miller, E.J.; Marqusee, S.
The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms
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391
450-460
2009
Escherichia coli
Connell, K.B.; Horner, G.A.; Marqusee, S.
A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble
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391
461-470
2009
Escherichia coli (P0A7Y4), Escherichia coli
Kauffmann, A.; Campagna, R.; Bartels, C.; Childs-Disney, J.
Improvement of RNA secondary structure prediction using RNase H cleavage and randomized oligonucleotides
Nucleic Acids Res.
37
e121
2009
Escherichia coli
Beilhartz, G.; Goette, M.
HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors
Viruses
2
900-926
2010
Escherichia coli, Homo sapiens
Babu, C.S.; Dudev, T.; Lim, C.
Differential role of the protein matrix on the binding of a catalytic aspartate to Mg2+ vs Ca2+: application to ribonuclease H
J. Am. Chem. Soc.
135
6541-6548
2013
Moloney murine leukemia virus (P03355), Escherichia coli (P0A7Y4)
Narayan, A.; Naganathan, A.N.
Evidence for the sequential folding mechanism in RNase H from an ensemble-based model
J. Phys. Chem. B
118
5050-5058
2014
Escherichia coli (P0A7Y4), Thermus thermophilus (P29253)
Naka, K.; Koga, M.; Yonesaki, T.; Otsuka, Y.
RNase HI stimulates the activity of RnlA toxin in Escherichia coli
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91
596-605
2014
Escherichia coli
Moelling, K.; Broecker, F.; Russo, G.; Sunagawa, S.
RNase H as gene modifier, driver of evolution and antiviral defense
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8
1745
2017
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Escherichia coli (P0A7Y4)
Plashkevych, O.; Li, Q.; Chattopadhyaya, J.
How RNase HI (Escherichia coli) promoted site-selective hydrolysis works on RNA in duplex with carba-LNA and LNA substituted antisense strands in an antisense strategy context?
Mol. Biosyst.
13
921-938
2017
Escherichia coli
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