3.1.26.4: ribonuclease H
This is an abbreviated version!
For detailed information about ribonuclease H, go to the full flat file.
Word Map on EC 3.1.26.4
-
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
- 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
Reaction
Endonucleolytic cleavage to a 5'-phosphomonoester =
Synonyms
Ape-RNase HII, aRNase HII, Bh ribonuclease H, BhRNase H, CtepRNH, EcRNH, endoribonuclease H, endoribonuclease H (calf thymus), ERNH, huRNaseH1, hybrid nuclease, hybrid ribonuclease, hybridase, hybridase (ribonuclease H), KOD1, LC9-RNase H1, lmo1273, LRNase HII, More, nuclease, hybrid ribo-, nuclease, ribo-, H, P32, protein ST0753, reverse transcriptase, ribonuclease H, ribonuclease H I, ribonuclease H(42), ribonuclease H(70), ribonuclease H1, ribonuclease H2, ribonuclease H3, ribonuclease HI, ribonuclease HII, ribonuclease HIII, ribonulease H1, RNA*DNA hybrid ribonucleotidohydrolase, RNA*DNA hybrid ribonucleotiohydrolase, RNase H, RNase H type 2, RNase H(35), RNase H1, RNase H2, RNase H3, RNase HI, RNase HII, RNase HIII, RNaseH, Rnaseh1, RNASEH2A, RNH, RNH1, RNH2, rnhA, RnhB, rnhC, rnhD, Rv2228c, ST0519, STK_07530, Sto-RNase HI, T4 RNase H, Tk-RNase HII, Tk-Tk-RNase HII, TK0805, TRNH, TthRNH, Ty1 reverse transcriptase/RNase H, type 1 ribonuclease H, type 1 RNase H, type 2 ribonuclease H, type 2 RNase H, type II ribonuclease H
ECTree
3.1.26.4 ribonuclease HAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.1.26.4 - ribonuclease 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
(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*DNA + H2O
?
Tequatrovirus T4
-
5'-to 3'-exonuclease activity, degradation of DNA*DNA duplexes
-
-
?
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-2'-methoxyethoxy RNA hybrid
?
-
chimeric substrates containing a central DNA region with flanking northern-biased 2'-methoxyethyl nucleotides hybridized to complementary RNA, enhanced cleavage rates are observed for the eastern-biased 2'-ara-fluorothymidine and bulge inducing N-methylthymidine modifications positioned at the 5'-DNA/3'-MOE junction as well as the southern-biased 2'-methylthiothymidine and conformationally flexible tetrafluoroindole modifications positioned at the 5'-MOE/3'-DNA junction, overview
-
-
?
DNA-2'-methoxyethoxy-antisense RNA hybrid + H2O
?
-
2'-methoxyethoxy nucleotides, positioned at the 3' and 5' poles, into the antisense oligodeoxyribonucleotide of the heteroduplex to alter the helical geometry of the substrate
-
-
?
DNA-rN1-DNA/DNA + H2O
?
-
specific cleavage by RNase HII at the 5'-side of the ribonucleotide, cleavage efficiencies of the perfectly matched DNA-rN1-DNA/DNA duplexes are higher than those carrying a mismatched ribonucleotide
-
-
?
DNA-RNA hybrid + H2O
ssDNA + 5'-phosphomonoester oligonucleotides
-
in the pause of minus strang synthesis, RNAse H degrades the RNA template, with the exception of the polypurine tract sequence, immediately upstream of U3, which serves as a primer for plus-strand synthesis
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
DNA-RNA-DNA/DNA hybrid + H2O
?
a duplex containing a (5')RNA-DNA(3') junction with one, three, or six ribonucleotides, i.e. DNA5-RNA1-DNA6/DNA12, DNA3-RNA3-DNA6/DNA12, and RNA6-DNA6/DNA12, and a substrate with a (5')DNA-RNA(3') junction, DNA5-RNA7/DNA12
-
-
?
DNA12-RNA1-DNA27/DNA40 hybrid + H2O
?
-
enzyme cleaves RNA20/DNA20 hybrid and DNA12-RNA1-DNA27/DNA40 hybrid substrates with similar efficiency
-
?
dsDNA oligonucleotide with a single ribose + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
dsDNA oligonucleotide with a stretch of ribonucleotides + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
-
enzyme excises misincorporated ribonucleotides in DNA
-
-
?
dsDNA oligonucleotides with a single ribose + H2O
dsDNA oligonucleotides with 1 nt gap + 5'-monophosphate ribonucleotide
-
preferred substrate, enzyme excises misincorporated ribonucleotides in DNA, enzyme places the first 5' nick, while the second 3' cut is made by Rad27p
-
-
?
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
?
-
-
-
-
?
peptide nucleic acid - 2'-deoxy 2'-fluoroarabinonucleic acid hybrid + H2O
?
-
chimeric oligomers possessing a single central peptide nucleic acid insert are capable of forming hybrid duplexes with complementary RNA, although with diminished thermal stability in comparison to the unmodified oligomers
-
-
?
peptide nucleic acid - DNA + H2O
?
-
chimeric oligomers possessing a single central peptide nucleic acid insert are capable of forming hybrid duplexes with complementary RNA, although with diminished thermal stability in comparison to the unmodified oligomers
-
-
?
poly-rA/poly-dT + H2O
?
-
products are short oligonucleotides with very few intermediate-sized oligonucleotides
-
?
RNA*DNA hybrid + H2O
5'-phospho-3'-hydroxyoligonucleotides
-
specifically degrades the RNA moiety
-
-
?
RNA*DNA hybrid + H2O
DNA + 5'-phosphonucleotides
Tequatrovirus T4
-
5'-to 3'-exonuclease activity, degradation of RNA*DNA duplexes
-
-
?
RNA-DNA heteroduplex + H2O
?
the enzyme digests an RNA-RNA duplex in the presence of Mn2+
-
-
?
RNA-DNA hybrid HTS-1 + H2O
?
5'-GAUCUGAGCCUGGGAGCU-fluorescein-3' annealed to 5'-Dabcyl-AGCTCCCAGGCTCAGATC-3'
-
-
?
RNA-DNA hybrid HTS-2 + H2O
?
5'-CUGGUUAGACCAGAUCUGAGCCUGGGAGCU-fluorescein-3' annealed to 5'-Dabcyl-AGCTCCCAGGCTCAGATC-3'
-
-
?
RNA-DNA*DNA hybrid + H2O
8mer oligonucleotide
7 M urea-denatured 18mer, no activity with untreated hybrid, specific removal of the RNA portion of the duplex
-
-
?
RNA-DNA*DNA hybrid + H2O
oligonucleotides
7 M urea-denatured 37mer, no activity with untreated hybrid, specific removal of the RNA portion of the duplex
a 20mer, a 10mer, a 9mer, and a 7mer
-
?
RNA-DNA/DNA hybrid + H2O
?
-
PabRNase HII acts as a specific endonuclease on RNA-DNA/DNA duplexes. Specific cleavage, one nucleotide upstream of the RNA-DNA junction, occurs on a substrate in which RNA initiators is fully annealed to the cDNA template. Additionally, PabRNase HII cleaves a single ribonucleotide embedded in a double-stranded DNA
-
-
?
RNA20/DNA20 hybrid + H2O
?
-
enzyme cleaves RNA20/DNA20 hybrid and DNA12-RNA1-DNA27/DNA40 hybrid substrates with similar efficiency
-
?
single-stranded RNA + H2O
?
-
isoenzyme C-1 and C-2 specifically act on the RNA moiety of RNA-DNA hybrid, isoenzyme C-3 degrades single-stranded RNA as well as the RNA of hybrids
-
-
?
ssDNA-dsDNA + H2O
?
Tequatrovirus T4
-
5'-to 3'-exonuclease activity, exonuclease activity removing short oligonucleotides of 3-30 nucleotides from adjacent DNA
-
-
?
[(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
?
-
-
-
-
?
12 base pair RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
-
?
12 base pair RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
12 base pair RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
12 basepair DNA-DNA duplex + H2O
?
oligomeric substrate, cleavage at multiple sites, product identification
-
-
?
12 basepair DNA-DNA duplex + H2O
?
-
oligomeric substrate, cleavage at multiple sites, product identification
-
-
?
12bp-RNA-DNA hybrid + H2O
?
-
RNase HII cleaves the 12 bp RNA-DNA substrate at multiple sites, but RNase HIII at only one site
-
-
?
12bp-RNA-DNA hybrid + H2O
?
-
RNase HII cleaves the 12 bp RNA-DNA substrate at multiple sites, but RNase HIII at only one site
-
-
?
29 basepair DNA-RNA-DNA/DNA + H2O
?
oligomeric substrate, cleavage mainly in the middle of the tetraribonucleotide, product identification
-
-
?
29 basepair DNA-RNA-DNA/DNA + H2O
?
-
oligomeric substrate, cleavage mainly in the middle of the tetraribonucleotide, product identification
-
-
?
5'-(6-carboxy-fluorescein)-cggagaugacgg-3'/5'-CCGTCTCTCCG-3' + H2O
?
the enzyme cleaves 12-bp RNA/DNA at multiple sites between the 3rd and 11th residues, but most preferentially at c10g11 and less preferentially at g5a6 and u7g8. The cleavage pattern of Mg2+-dependent activity is the same as that of Co2+-dependent activity, but different from that of Mn2+-dependent activity
-
-
?
5'-(6-carboxy-fluorescein)-cggagaugacgg-3'/5'-CCGTCTCTCCG-3' + H2O
?
the enzyme cleaves 12-bp RNA/DNA at multiple sites between the 3rd and 11th residues, but most preferentially at c10g11 and less preferentially at g5a6 and u7g8. The cleavage pattern of Mg2+-dependent activity is the same as that of Co2+-dependent activity, but different from that of Mn2+-dependent activity
-
-
?
DNA-RNA duplex + H2O
?
-
the enzyme cleaves RNA exclusively in a DNA-RNA heteroduplex, cleavage pattern and site specificity dependent on the substrate structure, overview
-
-
?
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 + H2O
DNA + 5'-phosphonucleotides
-
-
-
?
DNA-RNA hybrid + H2O
DNA + 5'-phosphonucleotides
3H-labeled M13 DNA/RNA hybrid substrate, the N-terminal domain and C-terminal helix are involved in substrate binding, but the former contributes to substrate binding to a higher extent than the latter, overview
-
-
?
DNA-RNA hybrid + H2O
DNA + 5'-phosphonucleotides
-
-
-
-
?
DNA-RNA hybrid + H2O
DNA + 5'-phosphonucleotides
-
strategy for regulating RNA digestion by RNase H by using a light-activated DNA hairpin, overview
-
-
?
DNA-RNA hybrid + H2O
DNA + 5'-phosphonucleotides
-
poly-rA/poly-dT substrate, RNase H1 contains an N-terminal domain termed dsRHbd or hybrid binding domain for binding both dsRNA and RNA/DNA hybrid, the RNA strand is recognized by a protein loop, which forms hydrogen bonds with the 2'-OH groups, substrate recognition and binding structure, residues, Y29, R32, R33, W43, R57, K59, K60, R72, and K73 are involved, overview
determination of reaction products with less than 20-nucleotides
-
?
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
-
?
DNA-RNA-DNA hybrid + H2O
?
-
specific hydrolysis of the RNA strand of the hybrid
-
-
?
DNA-RNA-DNA hybrid + H2O
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
specific hydrolysis of the RNA strand of the hybrid
-
-
?
dsDNA oligonucleotide with a single ribose + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
-
preferred substrate, enzyme excises misincorporated ribonucleotides in DNA
-
-
?
dsDNA oligonucleotide with a single ribose + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
-
enzyme excises misincorporated ribonucleotides in DNA, enzyme places the first 5' nick, while the second 3' cut is made by FEN-1 protein
-
-
?
dsDNA oligonucleotide with a single ribose + H2O
dsDNA oligonucleotide with 1 nt gap + 5'-monophosphate ribonucleotide
-
enzyme excises misincorporated ribonucleotides in DNA
-
-
?
M13 DNA-RNA hybrid + H2O
?
-
the enzyme degrades the RNA moiety of the heteroduplex
-
-
?
M13 DNA/RNA hybrid + H2O
?
substrate is 3H-labeled M13 DNA/RNA hybrid
-
-
?
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
-
-
?
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 + H2O
?
the enzyme cleaves the RNA strand of an RNA/DNA hybrid or an RNA/RNA duplex in the presence of Mn2+ or Co2+
-
-
?
RNA + H2O
?
the enzyme cleaves the RNA strand of an RNA/DNA hybrid or an RNA/RNA duplex in the presence of Mn2+ or Co2+
-
-
?
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*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*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
?
12 bp and 29 bp oligomers, cleavage site specificity depends on bound metal ion, wild-type end mutant enzymes
-
-
?
RNA*DNA hybrid + H2O
?
-
enzyme is active only under reducing conditions, wild-type enzyme and deletion mutant H1[DELTA1-73] are inactive under oxidizing conditions
-
-
?
RNA*DNA hybrid + H2O
?
-
the C-terminal domain of type 2 enzyme is involved in the interaction with the substrate
-
-
?
RNA*DNA hybrid + H2O
?
-
hydrolyses the RNA strang of the RNA*DNA heteroduplex
-
-
?
RNA-DNA duplex + H2O
?
substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain
-
-
?
RNA-DNA duplex + H2O
?
substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain
-
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme could be involved in the removal of RNA primers during DNA replication
-
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme may play a role in ribonucleotide excision from genomic DNA during replication
-
-
?
RNA-DNA hybrid + H2O
?
RNases H3 recognizes the 2'-OH groups of the RNA strand and detects the DNA strand by binding a phosphate group and inducing B-form conformation
-
-
?
RNA-DNA hybrid + H2O
?
RNases H3 recognizes the 2'-OH groups of the RNA strand and detects the DNA strand by binding a phosphate group and inducing B-form conformation
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
DNA-RNA hybrid made from phage f1 DNA
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
DNA-RNA hybrid made from phage f1 DNA
the bulk of the resulting poly(dA) obtained by cleavage of poly(dT)*poly(A4)-(dA)x still retains one covalently linked riboadenylic acid end group, a small portion carries a ribo dinucleotide
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
deoxyribotetranucleotides can still be cleaved
the bulk of the resulting poly(dA) obtained by cleavage of poly(dT)*poly(A4)-(dA)x still retains one covalently linked riboadenylic acid end group, a small portion carries a ribo dinucleotide
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
oligoribonucleotides + monoribonucleotides terminated by a 5'-phosphate
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(dT)'poly(A) in the presence of Mg2+ is the best substrate, poly(dC)'poly(G) is attacked much more slowly. Degradation velocity rises with the increasing length of the deoxyribo strand. The efficieny decreases in the following order: (dA)4-poly(U), (dG)4*poly(C), (dC)4*poly(G), (dT)4*poly(A)
the bulk of the resulting poly(dA) obtained by cleavage of poly(dT)*poly(A4)-(dA)x still retains one covalently linked riboadenylic acid end group, a small portion carries a ribo dinucleotide
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
a mixture of oligoribonucleotides with 5'-phosphate and 3'-hydroxyl terminus, oligonucleotides of various chain length, mainly 3-9 nucleotides in length
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
a mixture of oligoribonucleotides with 5'-phosphate and 3'-hydroxyl terminus, oligonucleotides of various chain length, mainly 3-9 nucleotides in length
?
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
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
a mixture of oligoribonucleotides with 5'-phosphate and 3'-hydroxyl terminus
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
the enzyme can hydrolyze a DNA*RNA*DNA/DNA heteroduplex that contains a single ribonucleotide
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
hybrid obtained by transcription of calf thymus DNA
oligoribonucleotides with 3'-OH and 5'-phosphate ends
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
oligoribonucleotides with 3'-OH and 5'-phosphate ends
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
isoenzyme C-1 and C-2 specifically act on the RNA moiety of RNA-DNA hybrid, isoenzyme C-3 degrades single-stranded RNA as well as the RNA of hybrids
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(dCrI)
oligoribonucleotides with a chain length of less than 15, having 5'-phosphate and 3'-hydroxyl end group, oligonucleotides of chain length 6-14, no mononucleotides formed
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rUdA)
oligoribonucleotides with 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
oligoribonucleotides with a chain length of less than 15, having 5'-phosphate and 3'-hydroxyl end group, oligonucleotides of chain length 6-14, no mononucleotides formed
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
oligonucleotides with 3'-hydroxyl and 5'-phosphate termini with the structure (pA)3-9 are formed from poly(A)*poly(dT)
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
a mixture of oligonucleotides with 5'-phosphate termini and only a minor proportion of 5'-mononucleotide
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
T7 DNA-RNA hybrids
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rCdG)
mixture of oligonucleotides, ranging in size from dinucleotides to larger than hexanucleotides. No mononucleotides can be detected
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
M13 DNA:RNA[P*]DNA
oligoribonucleotides with 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rUdA)
5'-phosphorylated oligonucleotides
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rCdI)
5'-phosphorylated oligonucleotides
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
mixture of oligonucleotides, ranging in size from dinucleotides to larger than hexanucleotides. No mononucleotides can be detected
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rAdT)
5'-phosphorylated oligonucleotides
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
RNase H2 incises the DNA 5'-of the ribonucleotide, generating DNA containing 3'-hydroxyl and 5'-phosphoribonucleotide ends
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
oligonucleotides and a small amount of mononucleotides which possess 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
-
oligonucleotides and a small amount of mononucleotides which possess 3'-hydroxyl and 5'-phosphate termini
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
M13 DNA/RNA hybrid
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
M13 DNA/RNA hybrid
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
can degrade about 90% of the RNA strand of and RNA-DNA hybrid
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
the enzyme specifically cleaves the RNA strand of RNA/DNA hybrids
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
Halalkalibacterium halodurans
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester + ?
-
-
-
?
RNA-DNA*DNA hybrid + H2O
DNA*DNA + 5'-phosphomononucleotides
RNA primer recognition and removal during DNA replication
-
-
?
RNA-DNA*DNA hybrid + H2O
DNA*DNA + 5'-phosphomononucleotides
Tequatrovirus T4
-
enzyme removes RNA primers from lagging strand fragments during DNA replication, 5'-to 3'-exonuclease activity, degradation of the RNA portion of the duplex
-
-
?
RNA-DNA*DNA hybrid + H2O
DNA*DNA + 5'-phosphomononucleotides
Tequatrovirus T4
-
specific removal of the RNA portion of the duplex
-
-
?
RNA-RNA duplex + H2O
?
substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain
-
-
?
RNA-RNA duplex + H2O
?
substrate both for full-lentgh enzyme and isolated RNase H N-terminal RNase H domain
-
-
?
RNA-RNA duplex + H2O
?
reaction occurs in presence of Mn2+-ions. Residues D110, R113 and F114 are responsible for the activity, the residues are located in the region that discriminates DNA from RNA in the non-substrate strand of the duplexes
-
-
?
RNA-RNA duplex + H2O
?
weak activity. Amino acid residues Asp110, Arg113 and Phe114 of RNase HII are strongly involved in the dsRNA-digestion activity of the enzyme
-
-
?
RNA/DNA hybrid + H2O
?
model Okazaki fragment 18-mer RNA-DNA/DNA substrate (Q18), RNase H is a structure-specific endonuclease, it cleaves the 25-bp RNA/DNA hybrid at multiple sites, indicating that the enzyme cleaves RNA/DNA in a sequence-independent manner. In the absence of complementary DNA, the chimeric RNA-DNA strand is not cleaved by the enzyme
-
-
?
additional information
?
-
-
no activity on natural double-stranded or single-stranded DNA, or on single-stranded RNA
-
-
?
additional information
?
-
-
stage-specific expression of RNAse H1 isozymes with different substrate specificities and divalent cation requirements, claevage specificties, overview
-
-
?
additional information
?
-
-
development of a CpRNase HII-based method for activity assay and detection: DNA-rN1-DNA fragments are modified with a fluorophore at the 5'-end and a quencher at the 3'-end to generate molecular beacons, which hybridize with single-stranded DNA to be cleaved by CpRNase HII, the method is suitable for large-scale genotyping, overview
-
-
?
additional information
?
-
-
substrate specificity and involved active site residues of RNases HII and HIII, overview
-
-
?
additional information
?
-
-
the enzyme can cleave a DNA-rN1-DNA/DNA substrate (rN1, one ribonucleotide) in vitro, e.g. a RNA-DNA hybrid consisting of CGTCCCaCCGTGC and aucagaaaaAGAGCG strands (capital letters and small bold letters represent DNA and RNA, respectively)
-
-
?
additional information
?
-
-
the enzyme can cleave a DNA-rN1-DNA/DNA substrate (rN1, one ribonucleotide) in vitro, e.g. a RNA-DNA hybrid consisting of CGTCCCaCCGTGC and aucagaaaaAGAGCG strands (capital letters and small bold letters represent DNA and RNA, respectively)
-
-
?
additional information
?
-
-
substrate specificity and involved active site residues of RNases HII and HIII, overview
-
-
?
additional information
?
-
recombinant EcRNH produced as a soluble form in Escherichia coli shows enzymatic activity to cleave the 3'-O-P bond of RNA in a DNA-RNA duplex, producing 3'-hydroxyl and 5'-phosphate
-
-
?
additional information
?
-
-
recombinant EcRNH produced as a soluble form in Escherichia coli shows enzymatic activity to cleave the 3'-O-P bond of RNA in a DNA-RNA duplex, producing 3'-hydroxyl and 5'-phosphate
-
-
?
additional information
?
-
-
the enzyme cannot cleave the phosphodiester bond covalently linking ribonucleotides to DNA
-
-
?
additional information
?
-
-
substrate characterizationa and substrate specificity
-
-
?
additional information
?
-
substrate cleavage mode of the enzyme, cleavage site specificity
-
-
?
additional information
?
-
-
substrate cleavage mode of the enzyme, cleavage site 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
-
-
?
additional information
?
-
RNase H specifically hydrolyzes the RNA strand of RNA/DNA hybrids in the presence of divalent metal ions, such as Mg2+ and Mn2+
-
-
?
additional information
?
-
-
RNase H specifically hydrolyzes the RNA strand of RNA/DNA hybrids in the presence of divalent metal ions, such as Mg2+ and Mn2+
-
-
?
additional information
?
-
model for the complex between Bst-RNase H3 and RNA/DNA hybrid and substrate binding mechanism, overview
-
-
?
additional information
?
-
-
model for the complex between Bst-RNase H3 and RNA/DNA hybrid and substrate binding mechanism, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans
member of the nucleotidyl-transferase superfamily and endo-nucleolytically cleaves the RNA portion in RNA/DNA hybrids and removes RNA primers from Okazaki fragments. Enzyme binds RNA and DNA duplexes but is unable to cleave either
-
-
?
additional information
?
-
Halalkalibacterium halodurans
conformational changes upon DNA-RNA hybrid duplex substrate binding, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
RNase (H)binding induces conformational changes in RNA-DNA hybrid. RNase H distorts the DNA strand of the hybrid by rotating the phosphodiester backbone around nucleotide dA6 about 5 A x02into the nucleotide binding pocket. The superimposition of the 2 RNA-DNA hybrids shows the RNA strand has a relatively similar conformation, but the DNA strand has been distorted to significantly widen the major groove of the helix. This flexibility of the DNA strand likely plays a role in substrate recognition and discrimination
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-125
-
RNase (H)binding induces conformational changes in RNA-DNA hybrid. RNase H distorts the DNA strand of the hybrid by rotating the phosphodiester backbone around nucleotide dA6 about 5 A x02into the nucleotide binding pocket. The superimposition of the 2 RNA-DNA hybrids shows the RNA strand has a relatively similar conformation, but the DNA strand has been distorted to significantly widen the major groove of the helix. This flexibility of the DNA strand likely plays a role in substrate recognition and discrimination
-
-
?
additional information
?
-
-
DNA oligonucleotide (ODN)-directed RNA cleavage assays are conducted. Substrate specificity of the HBV RNaseH, overview. HBV RNaseH activity requires an DNA:RNA heteroduplex of 14 bp or more for efficient cleavage. The full-length HBV RNaseH efficiently cleaves the RNA when the ODN ranges from 20-14 nt, but little to no cleavage is observed with the 13mer. HBV RNaseH cannot cut RNA:RNA duplexes. The HBV RNaseH enzyme also shows 3'-5' exoribonuclease activity, Ec 3.1.13.2
-
-
?
additional information
?
-
-
the enzyme lacks double-stranded and single-stranded RNase and DNase activities. No hydrolysis of the DNA moiety of the RNA/DNA heteroduplex
-
-
?
additional information
?
-
-
presence of intrinsic cell-type specific factors affecting the activity and localization of type 2 enzyme
-
-
?
additional information
?
-
-
the enzyme is regulated by a unique redox switch formed by adjacent Cys147 and Cys148
-
-
?
additional information
?
-
-
formation of a disulfide bond, under oxidizing conditions, between Cys147 and Cys148 results in an inactive enzyme conformation
-
-
?
additional information
?
-
-
substrate characterization and substrate specificity
-
-
?
additional information
?
-
-
design of a light-activated DNA hairpin to control the RNase H-mediated hydrolysis of mRNA, overview
-
-
?
additional information
?
-
-
substrate specificity of RNase H1 with modifies heteroduplexes, overview
-
-
?
additional information
?
-
-
both modification by unlocked nucleic acids and 4'-C-hydroxymethyl-DNA gap insertions are compatible with RNase H activity when used sparingly. Multiple 4'-C-hydroxymethyl-DNA modifications are better tolerated by RNase H than multiple unlocked nucleic acid modifications in the gap
-
-
?
additional information
?
-
-
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids. A two-metal ion mechanism requires that metal ion A activates a water molecule as a nucleophile and moves towards ion B, bringing the nucleophile in close proximity to the scissile bond, while metal ion B destabilizes the substrate-enzyme interaction and lowers the energy barrier to product formation
-
-
?
additional information
?
-
-
the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency
-
-
?
additional information
?
-
the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency
-
-
?
additional information
?
-
-
the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency
-
-
?
additional information
?
-
-
substrate is [alpha-32P]ATP-labeled poly(rA)/poly(dT)
-
-
?
additional information
?
-
-
the DNA/RNA duplex SP hybrid is a substrate for the enzyme while the RP hybrid is not. Structure-activity relationship, and NMR analysis of structural features important for enzyme activity, overview. A fully RP BH3 DNA/RNA hybrid might not be a substrate for RNase H1, NMR structure. Structural analysis of stereoregular borano phosphate modifications
-
-
?
additional information
?
-
reconstitution of the replication cycle of L-strand synthesis in vitro using recombinant mitochondrial proteins and model OriL substrates: the process begins with initiation of DNA replication at OriL and ends with primer removal and ligation. RNase H1 partially removes the primer, leaving behind the last one to three ribonucleotides. These 5'-end ribonucleotides disturb ligation and are removed by Flap endonuclease 1 (FEN1)
-
-
?
additional information
?
-
-
reconstitution of the replication cycle of L-strand synthesis in vitro using recombinant mitochondrial proteins and model OriL substrates: the process begins with initiation of DNA replication at OriL and ends with primer removal and ligation. RNase H1 partially removes the primer, leaving behind the last one to three ribonucleotides. These 5'-end ribonucleotides disturb ligation and are removed by Flap endonuclease 1 (FEN1)
-
-
?
additional information
?
-
RNase H is a non-specific endonuclease which degrades selectively the RNA strand in DNA/RNA duplexes
-
-
?
additional information
?
-
RNase H1 is an RNase H enzyme capable of cleaving RNA-DNA hybrids. It can cleave hybrids that are down to approximately 6 nucleotides in length. The enzyme can also cleave Okazaki fragment-like structures, leaving approximately two ribonucleotides next to the RNA-DNA junction
-
-
?
additional information
?
-
RNaseH1-dependent antisense oligonucleotides (ASOs) activity in human cells, mechanism and regulation, overview
-
-
?
additional information
?
-
a label-free chemiluminescent (CL) aptasensor is used for the sensitive detection of RNase H activity based on hairpin technology. The specific hairpin structure is a DNA-RNA chimeric strand, which contains a streptavidin aptamer sequence and a blocked RNA sequence. RNase H can specifically recognize and cleave the RNA sequence of the DNA-RNA hybrid stem, liberating the streptavidin aptamer (SA, 5'-ATT GAC CGC TGT GTG ACG CAA CAC TCA AT-3') which can be accumulated by streptavidin-coated magnetic microspheres (SA-MP). Then the CL signal is generated due to an instantaneous derivatization reaction between the specific CL reagent 3,4,5-trimethoxyphenyl-glyoxal (TMPG) and the guanine (G) nucleotides in the SA aptamer, method optimization, overview
-
-
?
additional information
?
-
degradation of cleaved mRNA fragments by RNase H1-dependent antisense oligonucleotides (ASOs). Expression of a cytoplasm-localized mutant 7SL RNA that contains a partial U16 small nucleolar RNA (snoRNA) sequence and treatement with an RNase H1-dependent antisense oligonucleotide (ASO) simultaneously reduces both the nuclear U16 snoRNA and the cytoplasmic 7SL mutant RNA as early as 30 min after transfection in an RNase H1-dependent manner. Both the 5' and 3' cleavage products of the 7SL mutant RNA are accumulated in the cytoplasm. Some ASOs can rapidly reduce mature mRNAs without reducing pre-mRNA levels, overview
-
-
?
additional information
?
-
RNase H activated cleavage of ORN3-ORN6 by incoming ribonucleotides
-
-
?
additional information
?
-
RNase H1 can process mitochondrial R-loops. RNase H1 gradually degrades R-loops in a concentration-dependent manner, generating shorter RNA species. The shorter RNA species may be involved in hybrid G-quadruplex formation, and therefore partially resistant to RNase H1 degradation. With a template lacking L-strand promoter (LSP), RNase H1 has no apparent effects on DNA synthesis and no short DNA products are observed when RNase H1 is added together with mtSSB. Priming is dependent on R-loops, the presence of LSP. No DNA synthesis from processed LSP R-loops in the absence of RNase H1. Upon addition of RNase H1, replication products with sizes between 12 and 21 nts are observed. The highest levels of DNA synthesis are observed at 2 nM of RNase H1
-
-
?
additional information
?
-
RNase H1 cleaves RNA in RNA-DNA hybrids to generate free 3'-OH and 5'-phosphate groups. The enzyme requires substrates containing at least four ribonucleotides to be active. RNase H1 cuts only between ribonucleotides, leaving at least 2 ribonucleotides attached to the 5'-end of the DNA. Nuclease activity reactions are performed on an 80 nt DNA template annealed to a 3' end labelled 52 nt chimeric oligonucleotide that contains 26 ribonucleotides followed by 26 deoxyribonucleotides (26RNA:26DNA)
-
-
?
additional information
?
-
-
RNase H1 cleaves RNA in RNA-DNA hybrids to generate free 3'-OH and 5'-phosphate groups. The enzyme requires substrates containing at least four ribonucleotides to be active. RNase H1 cuts only between ribonucleotides, leaving at least 2 ribonucleotides attached to the 5'-end of the DNA. Nuclease activity reactions are performed on an 80 nt DNA template annealed to a 3' end labelled 52 nt chimeric oligonucleotide that contains 26 ribonucleotides followed by 26 deoxyribonucleotides (26RNA:26DNA)
-
-
?
additional information
?
-
the enzyme is required for kinetoplast DNA replication in the mitochondrion, the RNase HIIC is essential for growth of promastigotes and amastigotes
-
-
?
additional information
?
-
the enzyme is required for kinetoplast DNA replication in the mitochondrion, the RNase HIIC is essential for growth of promastigotes and amastigotes
-
-
?
additional information
?
-
-
no activity with dT36 and polyA
-
-
?
additional information
?
-
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
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additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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-
?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
-
RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
-
-
?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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-
?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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-
?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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-
?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes
-
-
?
additional information
?
-
-
RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
-
-
?
additional information
?
-
RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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-
?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H2 is uniquely capable of incising a single embedded rNMP. Substrate specificity, overview
-
-
?
additional information
?
-
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
-
-
?
additional information
?
-
RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
-
-
?
additional information
?
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RnhC like RnhA is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA
-
-
?
additional information
?
-
-
RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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?
additional information
?
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RNase H enzymes incise the RNA strand of RNA:DNA hybrid duplexes. They are classified as type I (H1) or type II (H2 and H3). RNase H1 requires an oligoribonucleotide tract and is unable to incise a single ribonucleotide embedded in duplex DNA. Nucleis acid substrate specificity, minimal RNA requirement for RnhA, RnhA is a canonical type I RNase H enzyme, overview. Cleavage of chimeric RNA-DNA strands by RnhA. RnhA does not preferentially cleave the junctions of RNA and DNA segments, and RnhA does not completely remove a ribonucleotide tract installed 3' of DNA to yield a clean DNA3'OH end. RnhA does not incise the 32P-labeled RNA single strand
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additional information
?
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ribonuclease H(70) possesses cryptic reverse transcriptase activity
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additional information
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ribonuclease H(70) possesses cryptic reverse transcriptase activity
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additional information
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substrate specificity, enzyme plays a role in the repair of misincorporated ribonucleotides rather than or in addition to processing RNA*DNA hybrid molecules
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additional information
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substrate cleavage mode of the enzyme, cleavage site specificity
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additional information
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substrate cleavage mode of the enzyme, cleavage site specificity
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additional information
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RNases hydrolyze RNA/DNA in the presence of various divalent cofactors such as Mg2+ and Mn2+
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additional information
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RNases hydrolyze RNA/DNA in the presence of various divalent cofactors such as Mg2+ and Mn2+
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additional information
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the enzyme utilizes hybrid RNA/DNA as a substrate. Cleavage activity of RNase HII with different oligomeric substrates, overview
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additional information
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ribonuclease H is an enzyme that specifically cleaves RNA of RNA?DNA hybrids
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additional information
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RNase H2 hydrolyzes RNA of RNA/DNA hybrids and can nick duplex DNAs containing a single ribonucleotide. It shows a unique mechanism of recognition and substrate-assisted cleavage with preference for junction substrates. A conserved tyrosine residue distorts the nucleic acid at the junction, allowing the substrate to function in catalysis by participating in coordination of the active site metal ion
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additional information
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determination of cleavage-site specificity, overview
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