ArticleJournal of virology2000
Asymmetric subunit organization of heterodimeric Rous sarcoma virus reverse transcriptase alphabeta: localization of the polymerase and RNase H active sites in the alpha subunit.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Review
- Retroviral DNA Transposition: Themes and Variations.Microbiology spectrum · 2014Article
- Alternate polypurine tracts (PPTs) affect the rous sarcoma virus RNase H cleavage specificity and reveal a preferential cleavage following a GA dinucleotide sequence at the PPT-U3 junction.Journal of virology · 2005Article
- Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.Eukaryotic cell · 2005Article
- Functional roles of carboxylate residues comprising the DNA polymerase active site triad of Ty3 reverse transcriptase.Nucleic acids research · 2005Article
- The role of template-primer in protection of reverse transcriptase from thermal inactivation.Nucleic acids research · 2002Article
- Subcellular localization and integration activities of rous sarcoma virus reverse transcriptase.Journal of virology · 2002Article
- Ty3 integrase is required for initiation of reverse transcription.Journal of virology · 2002Article
- Requirements for minus-strand transfer catalyzed by Rous sarcoma virus reverse transcriptase.Journal of virology · 2001Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genes encoding the alpha (63-kDa) and beta (95-kDa) subunits of Rous sarcoma virus (RSV) reverse transcriptase (RT) or the entire Pol polypeptide (99 kDa) were mutated in the conserved aspartic acid residue Asp 181 of the polymerase active site (YMDD) or in the conserved Asp 505 residue of the RNase H active site. We have analyzed heterodimeric recombinant RSV alphabeta and alphaPol RTs within which one subunit was selectively mutated. When alphabeta heterodimers contained the Asp 181-->Asn mutation in their beta subunits, about 42% of the wild-type polymerase activity was detected, whereas when the heterodimers contained the same mutation in their alpha subunits, only 7.5% of the wild-type polymerase activity was detected. Similar results were obtained when the conserved Asp 505 residue of the RNase H active site was mutated to Asn. RNase H activity was clearly detectable in alphabeta heterodimers mutated in the beta subunit but was lost when the mutation was present in the alpha subunit. In summary, our data imply that the polymerase and RNase H active sites are located in the alpha subunit of the heterodimeric RSV RT alphabeta.
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