3.1.13.2: exoribonuclease H
This is an abbreviated version!
For detailed information about exoribonuclease H, go to the full flat file.
Word Map on EC 3.1.13.2
-
3.1.13.2
-
strand
-
duplex
-
nucleic
-
rna-dna
-
single-stranded
-
integrase
-
r-loops
-
oligodeoxynucleotides
-
retrotransposons
-
heteroduplexes
-
transcriptases
-
phosphorothioate
-
retroviruses
-
polypurine
-
moloney
-
phosphodiester
-
exonuclease
-
rna-dependent
-
pre-mrnas
-
nucleases
-
oligodeoxyribonucleotides
-
plus-strand
-
nnrti
-
template-primer
-
nucleocapsids
-
minus-strand
-
dntp
-
spliceosome
-
myeloblastosis
-
thumb
-
endonucleolytic
-
oligonucleotide-directed
-
2'-o-methylated
-
nevirapine
-
snrnp
-
oligoribonucleotide
-
primer-template
-
okazaki
-
nonnucleoside
-
rna-directed
-
a-form
-
efavirenz
-
retroelements
-
3'-exonuclease
-
heteropolymeric
-
phosphoramidite
-
pregenomic
-
hepadnavirus
-
hiv-rt
-
pharmacology
-
medicine
-
drug development
-
internucleotide
- 3.1.13.2
- strand
- duplex
- nucleic
- rna-dna
-
single-stranded
-
integrase
-
r-loops
- oligodeoxynucleotides
-
retrotransposons
- heteroduplexes
- transcriptases
- phosphorothioate
- retroviruses
-
polypurine
-
moloney
-
phosphodiester
-
exonuclease
-
rna-dependent
- pre-mrnas
- nucleases
- oligodeoxyribonucleotides
-
plus-strand
-
nnrti
-
template-primer
-
nucleocapsids
-
minus-strand
- dntp
-
spliceosome
-
myeloblastosis
-
thumb
-
endonucleolytic
-
oligonucleotide-directed
-
2'-o-methylated
- nevirapine
-
snrnp
- oligoribonucleotide
-
primer-template
-
okazaki
-
nonnucleoside
-
rna-directed
-
a-form
- efavirenz
-
retroelements
- 3'-exonuclease
-
heteropolymeric
-
phosphoramidite
-
pregenomic
-
hepadnavirus
- hiv-rt
- pharmacology
- medicine
- drug development
-
internucleotide
Reaction
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid =
Synonyms
3'-to-5' RNase H, HIV RNase H, HIV-1 ribonuclease H, HIV-1 RT ribonuclease H, LC11-RNase H1, More, Prp8, retroviral reverse transcriptase RNaseH, retroviral RNase H, reverse transcriptase ribonuclease H, reverse transcriptase-associated ribonuclease H, ribonuclease H, RNase H, RNase H1, RNase HI, RNaseH, RNH, RNH1, RT RNase H, RT/RNase H, T4 RNase H, Ta11
ECTree
3.1.13.2 exoribonuclease HAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.1.13.2 - exoribonuclease H
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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
18mer DNA-RNA hybrid + H2O
?
-
the RNA is labeled with 6-carboxytetramethyl rhodamine at the 3' end and annealed to complementary nonlabeled DNA
-
-
?
3' end-labeled 41-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
the most RNA fragments are cleaved by a combination of primary, secondary primary, and 5-nt cuts
?
5' end-labeled 41-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
The first product observed is the primary cut. The primary cut occurs faster than the secondary cut
?
5' end-labeled 50-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
The first product observed is the primary cut. The primary cut occurs faster than the secondary cut
?
5' end-labeled RNA
RNA fragments
-
cleavage of 267 nt RNA substrate to produce a 47 nt long product, the second cleavage produces RNA fragments that are 38 nt long
-
?
5' RNA-DNA duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
?
CGK1 + H2O
?
-
RNase H substrate CGK1 is obtained by annealing 5'-cap-labelled R1 5'-m7Gppp*GmAAUACUCAAGCUAUGCAUC-3' with DNA oligonucleotide D1. The RNA oligonucleotide is blocked at the 5' end by adding a guanosyl-5'-5'-guanosine triphosphate cap structure
-
-
?
DNA-RNA hybrid + H2O
DNA nucleotides + RNA nucleotides
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rGdC)
-
-
?
12 bp RNA/DNA hybrid + H2O
?
-
5'-(6-carboxyfluorescein)-labeled 12 base RNA (5'-cggagaugacgg-3') is hybridized with with a 1.5 M equivalent of the complementary DNA
-
-
?
12 bp RNA/DNA hybrid + H2O
?
-
5'-(6-carboxyfluorescein)-labeled 12 base RNA (5'-cggagaugacgg-3') is hybridized with with a 1.5 M equivalent of the complementary DNA
-
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
DNA-RNA hybrid + H2O
?
Avian sarcoma leukosis virus
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site specificity at -17, -12 and -8 from the 5' end positions of the RNA strand in 3' to 5' direction, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
formed by commercial R1 RNA and D1 DNA oligonucleotides, the His-tag affects the cleavage pattern of recombinant RNaseh domain
-
-
?
DNA-RNA hybrid + H2O
?
-
RNA-DNA hybrid structures: thermodynamics of recognition and impact on reverse viral replication
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage pattern to 3' end of wild-type and mutant reverse transcriptase/RNase H, HIV-1 reverse transcriptase employs the DNA 3' end-directed primary/secondary RNase H cleavage mechanism during synthesis and strand transfer
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site recognition and specificity, mechanism, in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
fluorescent-labeled RNA-DNA duplex of 15, 16, 17, or 18 nucleotide-RNA and in each case 18 nucleotide-DNA, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
RNA-DNA hybrid structures: thermodynamics of recognition and impact on reverse transcriptase-mediated RNase H activity, cleavage sites
-
-
?
DNA-RNA hybrid + H2O
?
-
substrate preparation, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
recessed 5'-end RNA substrates CGK1 annealed from RNA R1, i.e. 5'-GAAUACUCAAGCUAUGCAUC-3', and DNA D1, i.e. 5'-GATGCATAGCTTGAGTATTCTATAGTGAGTCGTATTAA-3', substrate labeling with fluorescein at the 3' end and with dabcyl at the 5' end
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H specifically hydrolyzes the RNA strand of a RNA/DNA heteroduplex, the ribonuclease H hydrolytic activity is part of the reverse transcriptase
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNaseH activity of HIV-1 reverse transcriptase cleaves the viral genome concomitant with minus strand synthesis during pausing of the reverse transcriptase activity, RNase H cleavage on a hairpin containing RNA template system, overview, pause-related 3' end-directed secondary cuts decreased primer extendibility, relationship between cleavage of the RNA template and extension of a DNA primer, mechanism, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H cleaves precisely one nucleotide from the tRNA/DNA junction, leaving a ribo-A on the 3' end of the viral minus-strand DNA
-
-
?
DNA-RNA hybrid + H2O
?
-
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 18 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H specifically hydrolyzes the RNA strand of a RNA/DNA heteroduplex, the ribonuclease H hydrolytic activity is part of the reverse transcriptase
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site recognition and specificity, mechanism, in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
sequence preference for internal cleavage. 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
DNA-RNA hybrid + H2O
?
-
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 19 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNase H primer grip is important for viral replication and replication fidelity, mutational analysis, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNase H catalytic efficiency and specificity is influences by the RNase H primer grip contacting the DNA primer strand and positioning the template strand near the RNase H active site, overview
-
-
?
DNA-RNA hybrid + H2O
?
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 19 base pair upstream from the 3' primer end
-
-
?
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
-
-
-
?
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
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
limited hydrolysis of ribopolymers when complementary DNA strand is missing or in presence of a complementary RNA strand
-
?
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
-
-
-
?
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
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
poor substrate: poly(rG)-poly(dC)
-
?
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
-
poor substrate: poly(rG)-poly(dC)
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Herpes simplex virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Herpes simplex virus HSV
-
-
-
?
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
-
-
-
?
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
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
only cleavage of RNA from a RNA-DNA-duplex
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
the RNase H domain of reverse transcriptase catalyses the cleavage of the RNA within DNA-RNA hybrids, both in a polymerase-dependent or independent fashion. Polymerase-dependent: Cleavage occurring at a distance of 18-20 nucleotides behind DNA polymerization. Polymerase-independent: cleavage of the viral RNA for the initiation of second DNA strand synthesis and for removal of the primer tRNA.
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
4-30 nucleotides in length
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
4-30 nucleotides in length
?
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
Rauscher leukemia virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Rauscher leukemia virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
RD-feline leukemia virus
-
-
-
?
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
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA/DNA + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, cleavage site selection modelling, RNase H activities of human retroviral reverse transcriptases preferentially cleave between two ribonucleotide residues in an RNA chain, and between the penultimate and last ribonucleotide of an extended RNA primer rather than precisely at the RNA-DNA junction, overview
-
-
?
DNA/DNA + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, RNase H activities of murine retroviral reverse transcriptases preferentially cleave between two ribonucleotide residues in an RNA chain, and between the penultimate and last ribonucleotide of an extended RNA primer rather than precisely at the RNA-DNA junction
-
-
?
double-stranded RNA + H2O
?
substrate of RNase H1
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
RNA/DNA hybrid + H2O
?
i.e. 18 nucleotide 3'-fluorescein-labeled RNA annealed to a complementary 18 nucleotide 5'-dabsyl-modified DNA, RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, substrate binding structure, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
RNA/DNA hybrid + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal,3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
secondary structure and substrate binding, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
additional information
?
-
-
not: poly(rU)-poly(dA), DNA-RNA hybrids without a free RNA-end
-
-
?
additional information
?
-
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
Avian sarcoma leukosis virus
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
additional information
?
-
-
heteroduplexes with 5'-O-methylphosphonate units in the antisense strand exhibit a significant increase in RNase H cleavage activity by up to 3fold in comparison with the natural heteroduplex
-
-
?
additional information
?
-
-
the 3'-5' exoribonuclease activity of the HBV RNaseH is determined. The enzyme also shows endolytic activity (EC 3.1.26.4) in DNA oligonucleotide (ODN)-directed RNA cleavage assays are conducted. Substrate specificity of the HBV RNaseH, overview
-
-
?
additional information
?
-
-
Herpes simplex virus 1 DNA polymerase shows also RNase H activity and acts in a 3'-to-5' direction, the activity is dependent on the 3'-to-5' exonuclease active site. No RNase H activity of HSV-1 DNA polymerase on RNA-DNA hybrids with 5' RNA termini
-
-
?
additional information
?
-
-
in vitro assays are performed utilizing purified wild-type Pol and the D368A exonuclease-deficient mutant, testing the ability of these enzymes to extend a fluorescently labeled DNA hairpin primer-template and degrade dsDNA and RNA-DNA hybrid hairpin substrates over time, assay of RNase H activity using differentially end-labeled templates with 5' or 3' RNA termini, e.g. 6-FAM-labeled hairpin RNA-DNA substrate with a 3' RNA terminus. Wild-type HSV Pol exhibits readily detectable RNase H activity on this substrate in the 3'-to-5' direction, while the mutant is inactive. Neither wild-type nor D368A Pol exhibits detectable RNase H activity on a substrate with a 5' RNA terminus
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase, RNase H substrate synthesis by the enzyme's RT activity
-
-
?
additional information
?
-
-
the isolated RNase H domain, part of reverse transcriptase, is catalytically active
-
-
?
additional information
?
-
-
in Mg2+, hydrolysis of poly(rAdT) appears to be solely endonucleolytic. In Mn2+, hydrolysis of poly(rAdT) is both endonucleolytic and exonucleolytic. With poly(rGdC) as substrate, hydrolysis is both endonucleolytic and exonucleolytic in either Mg2+ or Mn2+
-
-
?
additional information
?
-
-
the enzyme is essential for retroviral replication
-
-
?
additional information
?
-
-
the enzyme is essential to complete retroviral replication
-
-
?
additional information
?
-
-
the enzyme plays a key role in viral proliferation
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase residing on distinct domains of the enzyme with the DNA polymerase activity
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase, the isolated RNase H domain is inactive at low pH
-
-
?
additional information
?
-
-
the enzyme recognizes 3' ends of DNA and 5' ends of RNA for cleavage, the enzyme cleaves downstream of a nick, recognition of internal cleavage sites, influence of 5' end position of upstream RNA on cleavage of downstream RNA, overview
-
-
?
additional information
?
-
-
the reverse transcriptase possesses different activity domains and shows RNase H, integrase, and DNA polymerase activities
-
-
?
additional information
?
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
the RNase H function of HIV RT is required to effectively incorporate viral genetic information into the host cell genome
-
-
?
additional information
?
-
-
HIV reverse transcriptase, HIV-RT, contains two distinct protein domains catalyzing DNA polymerase and RNase H activities
-
-
?
additional information
?
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, the isolated RNase H domain of HIV-1 is inactive, but nuclease activity is reconstituted by introducing the p51 subunit, by adding the thumb and connection subdomains, or by various N-terminal fusions on the RNase H domain, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, the isolated RNase H domain of HIV-1 is inactive, but nuclease activity is reconstituted by introducing the p51 subunit, by adding the thumb and connection subdomains, or by various N-terminal fusions on the RNase H domain, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
the reverse transcriptase has two enzyme activities, one of which is the RNase H, enzyme-ligand interactions, overview
-
-
?
additional information
?
-
-
the reverse transcriptase has two enzyme activities, one of which is the RNase H, enzyme-ligand interactions, overview
-
-
?
additional information
?
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
additional information
?
-
-
cleaves RNA only if the RNA is part of an RNA/DNA duplex
-
-
?
additional information
?
-
-
during minus-strand DNA synthesis, RNase H degrades viral RNA sequences, generating potential plus-strand DNA primers
-
-
?
additional information
?
-
-
retroviral RNase H is essential for viral replication
-
-
?
additional information
?
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
-
RNA cleavage in the RNA-DNA hybrids by the various mutant HIV-2 reverse transcriptases, in comparison to the wild-type HIV-1 and HIV-2 reverse transcriptases
-
-
?
additional information
?
-
-
RNAse H is implicated in catalysing the degradation of the RNA strand during conversion of the viral genome into double-stranded DNA
-
-
?
additional information
?
-
the reverse transcriptase-associated RNase H activity introduces nicks into the RNA strand that yield low molecular weight bands in urea-containing denaturing PAGE, which are visualized by fluorescence scanning. The p51 preparation does not yield detectable low-molecular-weight bands, indicating that the reverse transcriptase preparation is not contaminated with RNase activities of bacterial origin
-
-
?
additional information
?
-
-
using specially designed RNA and DNA transfer substrates in vitro to determine how individual invasion sites contribute to the invasion-mediated mechanism of strand transfer, with specific focus on the limits and influences on the apparently crucial intermediate step of hybrid propagation. Investigation of the roles of the RNase H activities of reverse transcriptase and the strand-exchange properties of nucleocapsid protein (NC)
-
-
?
additional information
?
-
-
both of the enzymatic functions of reverse transcriptase, the DNA polymerase and RNase H, are essential for copying the single-stranded RNA genome found in virions into the double-stranded DNA that is inserted into the host genome by IN
-
-
?
additional information
?
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RNaseH assays are performed using an 18-nucleotide 3'-fluorescein-labeled RNA annealed to a complementary 18-nucleotide 5'-dabcyl-conjugated DNA. The increase in fluorescence as a result of RNase H hydrolysis is monitored with a Spectramax Gemini EM fluorescence spectrometer
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the RNase H function of HIV RT is required to effectively incorporate viral genetic information into the host cell genome
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RNA cleavage in the RNA-DNA hybrids by the various mutant HIV-2 reverse transcriptases, in comparison to the wild-type HIV-1 and HIV-2 reverse transcriptases
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the enzyme is essential for retroviral replication
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the enzyme is essential to complete retroviral replication
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the enzyme recognizes 3' ends of DNA and 5' ends of RNA for cleavage, the enzyme cleaves downstream of a nick, recognition of internal cleavage sites, influence of 5' end position of upstream RNA on cleavage of downstream RNA, overview
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mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
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mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
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the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
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the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
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3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
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retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
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retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
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RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
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RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
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LC11-RNase H1 does not exhibit double strand RNase activity
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LC11-RNase H1 does not exhibit double strand RNase activity
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LC11-RNase H1 does not exhibit double strand RNase activity
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Tequatrovirus T4
phage T4 RNase H shows 5'-3'exonuclease (EC 3.1.13.2) and flap endonuclease (EC 3.1.99.) activities on dsDNA
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