ArticleJournal of virology2001
A Ty1 reverse transcriptase active-site aspartate mutation blocks transposition but not polymerization.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.PLoS genetics · 2015Article
- The diversity of retrotransposons and the properties of their reverse transcriptases.Virus research · 2008Review
- Article
- Evolutionary pathways of the tirant LTR retrotransposon in the Drosophila melanogaster subgroup of species.Journal of molecular evolution · 2007Article
- Cooperation between reverse transcriptase and integrase during reverse transcription and formation of the preintegrative complex of Ty1.Eukaryotic cell · 2006Article
- Identification and characterization of critical cis-acting sequences within the yeast Ty1 retrotransposon.RNA (New York, N.Y.) · 2005Article
- An evaluation of detection methods for large lariat RNAs.RNA (New York, N.Y.) · 2005Article
- Functional roles of carboxylate residues comprising the DNA polymerase active site triad of Ty3 reverse transcriptase.Nucleic acids research · 2005Article
- Retrotransposons and their recognition of pol II promoters: a comprehensive survey of the transposable elements from the complete genome sequence of Schizosaccharomyces pombe.Genome research · 2003Article
- A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Reverse transcriptases (RTs) are found in a wide variety of mobile genetic elements including viruses, retrotransposons, and infectious organellar introns. An invariant triad of aspartates is thought to be required for the catalytic function of RTs. We generated RT mutants in the yeast retrotransposon Ty1, changing each of these active-site aspartates to asparagine or glutamate. All but one of the mutants lacked detectable polymerase activity. The novel exception, D(211)N, retained near wild-type in vitro polymerase activity within virus-like particles but failed to carry out in vivo transposition. For this mutant, minus-strand synthesis is impaired and formation of the plus-strand strong-stop intermediate is eliminated. Intragenic second-site suppressor mutations of the transposition defect map to the RNase H domain of the enzyme. Our results demonstrate that one of the three active-site aspartates in a retrotransposon RT is not catalytically critical. This implies a basic difference in the polymerase active-site geometry of Ty1 and human immunodeficiency virus RT and shows that subtle mutations in one domain can cause dramatic functional effects on a distant domain of the same enzyme.
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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.