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
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3.1.13.2
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strand
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duplex
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nucleic
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rna-dna
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single-stranded
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integrase
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r-loops
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oligodeoxynucleotides
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retrotransposons
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heteroduplexes
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transcriptases
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phosphorothioate
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retroviruses
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polypurine
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moloney
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phosphodiester
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exonuclease
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rna-dependent
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pre-mrnas
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nucleases
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oligodeoxyribonucleotides
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plus-strand
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nnrti
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template-primer
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nucleocapsids
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minus-strand
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dntp
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spliceosome
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myeloblastosis
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thumb
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endonucleolytic
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oligonucleotide-directed
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2'-o-methylated
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nevirapine
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snrnp
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oligoribonucleotide
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primer-template
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okazaki
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nonnucleoside
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rna-directed
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a-form
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efavirenz
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retroelements
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3'-exonuclease
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heteropolymeric
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phosphoramidite
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pregenomic
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hepadnavirus
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hiv-rt
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pharmacology
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medicine
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drug development
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internucleotide
- 3.1.13.2
- strand
- duplex
- nucleic
- rna-dna
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single-stranded
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integrase
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r-loops
- oligodeoxynucleotides
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retrotransposons
- heteroduplexes
- transcriptases
- phosphorothioate
- retroviruses
-
polypurine
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moloney
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phosphodiester
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exonuclease
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rna-dependent
- pre-mrnas
- nucleases
- oligodeoxyribonucleotides
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plus-strand
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nnrti
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template-primer
-
nucleocapsids
-
minus-strand
- dntp
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spliceosome
-
myeloblastosis
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thumb
-
endonucleolytic
-
oligonucleotide-directed
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2'-o-methylated
- nevirapine
-
snrnp
- oligoribonucleotide
-
primer-template
-
okazaki
-
nonnucleoside
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rna-directed
-
a-form
- efavirenz
-
retroelements
- 3'-exonuclease
-
heteropolymeric
-
phosphoramidite
-
pregenomic
-
hepadnavirus
- hiv-rt
- pharmacology
- medicine
- drug development
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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
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Engineering on EC 3.1.13.2 - exoribonuclease H
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D702A/E731A
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sequences encoding HBV RNaseH residues 809-844 are deleted from pMal-HRHgtC to create pMal-HRHgtCDELTA5. Active site residues D702 and E731 are mutated to alanines to create pMAL-HRHgtC(D702A/E731A) which encodes an inactive RNaseH
H264A
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the mutation causes an about 100fold decrease in kcat under multiple-turnover conditions, but does not alter the Km
D549N
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unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
E478Q
A360D
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mutation decreases the virus titer to about 50% of that of the wild-type virus
C280P
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mutation in either p66 or p51 subunits reduces RNase H activity in comparison to wild-type enzyme, the strand-transfer activity is very low
C280W
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mutation in either p66 or p51 subunits reduces RNase H activity in comparison to wild-type enzyme, the strand-transfer activity is very low
D358N
complete loss of Mg2+ and Mn2+-dependent RNase H activity
D426N
complete loss of Mg2+ and Mn2+-dependent RNase H activity
D469N
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
D549N
D67N/K70R/T215F/K219Q
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
E396A
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mutation decreases the virus titer to about 50% of that of the wild-type virus and has significant effect on the extent of enzyme cleavage
E401Q
complete loss of Mg2+ and Mn2+-dependent RNase H activity
E478Q
E89K
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site-directed mutagenesis, foscarnet-resistance mutation, the mutant enzyme shows different sensitivity for inhibitors compared to the wild-type enzyme, overview
G190A
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site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows reduced fitness compared to the wild-type enzyme
G190S
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site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows highly reduced fitness compared to the wild-type enzyme
G359S
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mutation decreases the virus titer to about 50% of that of the wild-type virus
H361A
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mutation decreases the virus titer to about 25% of that of the wild-type virus and affects the frequency of the generation of linear viral DNAs with aberrant ends
H427A
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
H539D
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site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
H539F
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site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
H539N
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site-directed mutagenesis, leads to a slowing down in the degradation of the RNA strand, decreases the frequency of reverse transcriptase template-switching by 2fold
H539R
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site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
K103N
K103N/Y181C
K390A
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mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
K395A
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mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
K476C
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the mutation disrupts the chemical cross-linking while maintaining activity
K65R
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nucleoside reverse transcriptase inhibitor resistance mutation
L74V
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nucleoside reverse transcriptase inhibitor resistance mutation
M184I
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nucleoside reverse transcriptase inhibitor resistance mutation
M41L/D67N/L210W/T215Y/A360V
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mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/A360V/N348I/E478Q
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mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/E478Q
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mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/N348I
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mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/N348I/A360V
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mutant accumulates transiently formed, shorter hybrids that can rebind to reverse transcriptase before the template is irreversibly degraded
P236L
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
Q151N
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nucleoside reverse transcriptase inhibitor resistance mutation
T362A
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mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
V106A
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
V106A/Y181C
Y181C
Y188L
Y459A
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
Y5014-(phenylcarbonyl)-L-Phe
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inserting a benzophenone into the RNase H primer grip (p66501BpF/p51 reverse transcriptase) creates an enzyme that is resistant to beta-thujaplicinol at inhibitor concentrations as high as 300 microM
Y5014-azido-L-Phe
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nonnatural amino acid substitution introducing an azido function
Y501A
complete loss of activity in comparison to wild-type enzyme
Y501Az-F
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p-azido-L-phenylalanine (Az-F), site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501Bp-F
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p-benzoyl-L-phenylalanine, site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501F
Y501G
complete loss of activity in comparison to wild-type enzyme
Y501H
complete loss of activity in comparison to wild-type enzyme
Y501L
complete loss of activity in comparison to wild-type enzyme
Y501Q
complete loss of activity in comparison to wild-type enzyme
Y501R
90% activity in comparison to wild-type enzyme, the mutant is completely resistant to N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone inhibition
Y501S
complete loss of activity in comparison to wild-type enzyme
Y501W
Q294Q/Q294R
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4.2fold RNase H activity compared to wild-type, Gln294 is modified in p54subunit, Q in p68, R in p54
D549N
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unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
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E478Q
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unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
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D599N/H742N
the RNase H activity of the mutant is seriously impaired
D224A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
D524A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
A558V
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site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus, reduced titer
Q559L
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site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus
S557A
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site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus, reduced titer
T590A
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site-directed mutagenesis, the mutation in the enzyme primer grip results in similar viral mutation rates compared to the wild-type enzyme/virus
Y586A
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site-directed mutagenesis, the mutant virus is not stable and cannot be expressed, no colonies
Y586F
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site-directed mutagenesis, the mutation in the enzyme primer grip results in 17fold increased viral mutation rates compared to the wild-type enzyme/virus
D1853A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
D1853N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
K1864E
prp8-D143, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D
prp8-151, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D/S1970R
prp8-152, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
R1937A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
R1937K
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1855A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1936A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1982A
prp8-153, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A, SA1966/7AG
prp8-154, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A,V1987A
prp8-155, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
V1870N
prp8-162, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
L242I
Tequatrovirus T4
naturally occuring mutation, the substitution does not affect the structure of RNase H and its role in providing the das-effect remains unclear
V43I
Tequatrovirus T4
naturally occuring mutation, the V43I substitution may lead to disposition of H4 helix, responsible for the interaction with the first base pairs of 5' end of branched DNA. These structural changes may affect unwinding of the first base pairs of gapped or nicked DNA generating a short flap and therefore may stabilize the DNA-enzyme complex
additional information
E478Q
-
unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
E478Q
-
site-directed mutagenesis, RNase H domain active site mutation, inactive mutant
D549N
-
have remarkable effects on viral replication by reducing the level of RNAse H activity
D549N
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site-directed mutagenesis, leads to a slowing down in the degradation of the RNA strand, decreases the frequency of reverse transcriptase template-switching by 2fold
E478Q
-
have remarkable effects on viral replication by reducing the level of RNAse H activity
E478Q
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RNase H-minus reverse transcriptase mutant. Comparison of the time course of 591R priming activity with wild type reverse transcriptase or an RNase H-minus reverse transcriptase mutant (E478Q) in the presence and absence of HIV-1 nucleocapsid protein (NC) to probe RNase H function
K103N
-
site-directed mutagenesis, NNRTI-resistance mutation, the mutant enzyme shows different sensitivity for inhibitors compared to the wild-type enzyme, overview
K103N
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
K103N
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
K103N
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site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows a fitness similar to the wild-type enzyme
K103N/Y181C
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site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
K103N/Y181C
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non-nucleoside reverse transcriptase inhibitor (NNRTI) resistant mutant
V106A/Y181C
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
V106A/Y181C
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non-nucleoside reverse transcriptase inhibitor (NNRTI) resistant mutant
Y181C
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
Y181C
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site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
Y181C
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
Y188L
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
Y188L
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
Y501F
85% activity in comparison to wild-type enzyme, the mutant remains sensitive to N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone inhibition
Y501F
-
site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501F
-
site-directed mutagenesis. IC50 for beta-thujaplicinol is comparable to wild-type value
Y501W
100% activity in comparison to wild-type enzyme, 6fold decreased sensitivity to inhibition N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone
Y501W
-
site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501W
-
site-directed mutagenesis. IC50 for beta-thujaplicinol is comparable to wild-type value
additional information
-
design of four Moloney murine leukaemia virus/Avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
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generation of a 3'-to-5' exonuclease-deficient mutant, D368A Pol. Wild-type and D368A mutant DNA polymerase exhibit similar polymerase activities, but the mutant enzyme is drastically impaired for 3'-to-5' exonuclease activity, with no activity detected even at high enzyme-to-DNA substrate ratios. The mutant shows no detectable ability to excise RNA with either a 3' or 5' terminus in contrast to the wild-type enzyme. Wild-type HSV Pol exhibits readily detectable RNase H activity on 6-FAM-labeled hairpin RNA-DNA substrate with a 3' RNA terminus 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
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deletion of the 3 C-terminal residues of RNase H domain leads to strong inhibition of RNA cleavage activity
additional information
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mutations of the RNase H domain of reverse transcriptase result in noninfectious virus particles
additional information
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
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mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
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identification of mutations in nucleoside reverse transcriptase inhibitor-treated patients. 3 mutations are found exclusively in nucleoside reverse transcriptase inhibitor-treated isolates. 9 mutations in the connection and 6 mutations in the RNase H are associated with nucleoside reverse transcriptase inhibitor treatment in subtype B. Some of them lay in or close to amino acid residues which contact nucleic acid or near the RNase H active site. Several of the residues have been recently associated to nucleoside reverse transcriptase inhibitor exposure or increase drug resistance to nucleoside reverse transcriptase inhibitor
additional information
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mutations in the C-terminus of HIV-1 reverse transcriptase, C-terminal reverse transcriptase mutations are resistant to both nucleoside analog reverse transcriptase inhibitor and nonnucleoside reverse transcriptase inhibitor. Other mutations are reviewed
additional information
mutations in the polymerase domain can affect RNase H activity by affecting the position of the template-primer or the structure of the RNase H domain itself. Aptamer inhibition of RNase H activity. Aptamer 12.01 and Aptamer M302 at varying concentrations (0, 50, 200, 1000 nM) are incubated with radiolabeled primer and an RNA template. Aptamers do not inhibit the RNase H activity of wild-type HIV-1 reverse transcriptase
additional information
-
mutations in the polymerase domain can affect RNase H activity by affecting the position of the template-primer or the structure of the RNase H domain itself. Aptamer inhibition of RNase H activity. Aptamer 12.01 and Aptamer M302 at varying concentrations (0, 50, 200, 1000 nM) are incubated with radiolabeled primer and an RNA template. Aptamers do not inhibit the RNase H activity of wild-type HIV-1 reverse transcriptase
additional information
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single methylphosphonate substitutions of the RNase H primer grip
additional information
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site-directed mutagenesis can affect the binding enzyme/substrate, resulting in a decrease in the RNAse H activity. Mutations in positions 448 and 505 have no effect on virus titre
additional information
-
TAMs refers to mutants that contain the following amino acid substitutions M41L/D67N/L210W/T215Y. Thymidine analogue-associated mutations (TAMs) in reverse transcriptase cause resistance to 3'-azido-3'-deoxythymidine (AZT) through excision of the incorporated monophosphate
additional information
the isolated HIV-1 RNase H domain is inactive, but the addition of various N-terminal extensions restores some RNase H activity. Changes at Trp266 and Phe61 in HIV-1 reverse transcriptase, both of which render the RNase H incapable of generating the polypurine tract (PPT) primer or removing the PPT primer once it has been extended primer grip residue Tyr501 in HIV-1 reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition
additional information
-
mutagenesis of Gln294 of the reverse transcriptase to find out how various amino acids, other that Gln and Pro at position 294 of HIV-2 reverse transcriptase affect the enzyme's RNase H activity. All modifications of HIV-2 reverse transcriptase Gln294 lead to an increase of the RNase H activity of the enzyme relative to the wild-type and also support the observations that residue 294 in the p54 subunit is the major contributor to the level of this activity in HIV-2 reverse transcriptase
additional information
-
construction of a mutant Mo-MLV RNase H lacking the putative helix C, surface mapping and substrate binding determinants, overview
additional information
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
isolated RNase H domain of Moloney murine leukemia virus reverse transcriptase is enzymatically active, but the activity is low and exhibits a greatly relaxed substrate specificity. Primer grip residue Tyr586 in Moloney murine leukemia virus reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition
additional information
all mutants are associated with dramatic growth defects and produced both cold- and temperature-sensitive phenotypes on mutation to asparagine
additional information
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all mutants are associated with dramatic growth defects and produced both cold- and temperature-sensitive phenotypes on mutation to asparagine
