ArticleJournal of virology1999
RNase H requirements for the second strand transfer reaction of human immunodeficiency virus type 1 reverse transcription.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Retroviral nucleocapsid proteins and DNA strand transfers.Biochimie open · 2018Review
- RNase H sequence preferences influence antisense oligonucleotide efficiency.Nucleic acids research · 2017Article
- Time-Resolved Imaging of Single HIV-1 Uncoating In Vitro and in Living Cells.PLoS pathogens · 2016Article
- Efavirenz stimulates HIV-1 reverse transcriptase RNase H activity by a mechanism involving increased substrate binding and secondary cleavage activity.Biochemistry · 2013Article
- Review
- HIV-1 reverse transcriptase dissociates during strand transfer.Journal of molecular biology · 2011Article
- Mechanism analysis indicates that recombination events in HIV-1 initiate and complete over short distances, explaining why recombination frequencies are similar in different sections of the genome.Journal of molecular biology · 2009Article
- RNase H activity: structure, specificity, and function in reverse transcription.Virus research · 2008Review
- Active site binding and sequence requirements for inhibition of HIV-1 reverse transcriptase by the RT1 family of single-stranded DNA aptamers.Nucleic acids research · 2007Article
- Increased G-->A transition frequencies displayed by primer grip mutants of human immunodeficiency virus type 1 reverse transcriptase.Journal of virology · 2004Article
- Human immunodeficiency virus type 2 reverse transcriptase activity in model systems that mimic steps in reverse transcription.Journal of virology · 2003Article
- Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein.Journal of virology · 2002Article
- Comparison of second-strand transfer requirements and RNase H cleavages catalyzed by human immunodeficiency virus type 1 reverse transcriptase (RT) and E478Q RT.Journal of virology · 2000Article
- Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer.Journal of virology · 2000Article
- Structural determinants of murine leukemia virus reverse transcriptase that affect the frequency of template switching.Journal of virology · 2000Article
- Impact of human immunodeficiency virus type 1 RNA dimerization on viral infectivity and of stem-loop B on RNA dimerization and reverse transcription and dissociation of dimerization from packaging.Journal of virology · 2000Article
- Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Retroviral reverse transcriptase (RT) enzymes are responsible for transcribing viral RNA into double-stranded DNA. An in vitro assay to analyze the second strand transfer event during human immunodeficiency virus type 1 (HIV-1) reverse transcription has been developed. Model substrates were constructed which mimic the viral intermediate found during plus-strand strong-stop synthesis. Utilizing wild-type HIV-1 RT and a mutant E478Q RT, the requirement for RNase H activity in this strand transfer event was analyzed. In the presence of Mg2+, HIV-1 RT was able to fully support the second strand transfer reaction in vitro. However, in the presence of Mg2+, the E478Q RT mutant had no detectable RNase H activity and was unable to support strand transfer. In the presence of Mn2+, the E478Q RT yields the initial endoribonucleolytic cleavage at the penultimate C residue of the tRNA primer yet does not support strand transfer. This suggests that subsequent degradation of the RNA primer by the RNase H domain was required for strand transfer. In reactions in which the E478Q RT was complemented with exogenous RNase H enzymes, strand transfer was supported. Additionally, we have shown that HIV-1 RT is capable of supporting strand transfer with substrates that mimic tRNAHis as well as the authentic tRNA3Lys.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.