3.1.26.13: retroviral ribonuclease H
This is an abbreviated version!
For detailed information about retroviral ribonuclease H, go to the full flat file.
Reaction
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
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Synonyms
HIV reverse transcriptase ribonuclease H, HIV reverse transcriptase-associated RNase H, HIV RNase H, HIV RT RNaseH, HIV RT-associated RNase H, HIV-1 reverse transcriptase, HIV-1 reverse transcriptase ribonuclease H, HIV-1 reverse transcriptase RNase H, HIV-1 RH, HIV-1 ribonuclease H, HIV-1 ribonuclease H domain, HIV-1 RNase H, HIV-1 RT-associated RNase H, human immunodeficiency virus reverse transcriptase, human immunodeficiency virus reverse transcriptase-associated ribonuclease H, human immunodeficiency virus reverse transcriptase-associated RNase H, human immunodeficiency virus RT-associated RNase H, M-MuLV RT RNase H, reverse transcriptase, reverse transcriptase-associated ribonuclease H, reverse transcriptase-associated RNase H, reverse-transcriptase-associated ribonuclease H, ribonuclease H, ribonuclease H domain in HIV-1 reverse transcriptase, RNase H, RNase H activity of HIV-1 reverse transcriptase, RNase H domain of HIV-1 reverse transcriptase, RNase H of HIV-1 subtype C, RNaseH, RNH, RNHHIV, RT RNase H, RT-RNase H
ECTree
Application
Application on EC 3.1.26.13 - retroviral ribonuclease H
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pharmacology
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mutations in RNase H can significantly contribute to drug resistance either alone or in combination with nucleoside reverse transcriptase inhibitor-resistance mutations in reverse transcriptase. There exists an equilibrium between nucleoside reverse transcriptase inhibitor incorporation, nucleoside reverse transcriptase inhibitor excision, and resumption of DNA synthesis and degradation of the RNA template by RNase H activity, leading to dissociation of the template-primer and abrogation of HIV-1 replication
analysis
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use of 6-phenylpyrrolocytidine as a sensitive fluorescent reporter group being non-disruptive to structure and the enzymatic activity of RNase H. A RNA/DNA hybrid possessing a single 6-phenylpyrrolocytidine insert is an excellent substrate for HIV-1 RT Ribonuclease H and rapidly reports cleavage of the RNA strand with a 14-fold increase in fluorescence intensity. The 6-phenylpyrrolocytidine-based assay for RNase H is superior to the traditional molecular beacon approach in terms of responsiveness, rapidity and ease. The assay is amenable to high-throughput microplate assay format
analysis
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use of a commercially available computed radiography system for dental radiography to produce images from radiolabeled polyacrylamide gel electrophoresis assays and its application for quantitative analyses of the human immunodeficiency virus type 1 reverse transcriptase polymerase-independent ribonuclease H activity monitored by PAGE analysis. The methodology allows quantifying effectively the RNase H catalyses and the obtained data are in good agreement with previous reference works
drug development
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the enzyme is a drug target
drug development
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RNase H activity is an attractive target for a new class of antiviral drugs
drug development
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the enzyme is a target for the development of effective dual HIV-1 IN and RNase H inhibitors
drug development
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the HIV RT-associated RNase H is avaluable drug target
medicine
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genotypical and statistical analyzes in HIV-1 reverse transcriptase from antiretroviral treatment-naive and antiretroviral treatment-experienced patients. Within the RNase H domain, change K451 is present in 11% of treatment-experienced patients, but not in treatment-naive patients
medicine
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively. A significant decline is observed in the viral loads of patients that are infected with HIV-1 carrying these substitutions and are subsequently treated with triple drug regimens, even in the case where zidovudine is included in such regimens. Generally, such single substitutions at the connection subdomain or RNase H domain have no influence on drug susceptibility in vitro by themselves. Instead, they generally enhance zidovudine resistance in the presence of excision-enhancing mutations. However, N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
medicine
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within the RNase domain, mutation K451R is present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients
medicine
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activating the RNase H prematurely inside the virus particles destroys the viral genome and abrogates viral infectivity
3.1.26.13 retroviral ribonuclease H
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