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Template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
During reverse transcription of the HIV-1 genome, two strand-transfer events occur. Both events rely on the RNase H cleavage activity of reverse transcriptases (RTs) and template homology. Using a panel of mutants of HIV-1(BH10) (group M/subtype B) and HIV-1(ESP49) (group O) RTs and in vitro assays,...
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| Pubblicato in: | J Biol Chem |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2018
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6120193/ https://ncbi.nlm.nih.gov/pubmed/29991591 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.004324 |
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