ArticleJournal of virology1996
Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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
31 citing papers in PubMed, 50 citations in OpenAlex.
- Advances in HIV-1 Assembly.Viruses · 2022Review
- The Oldest Co-opted gag Gene of a Human Endogenous Retrovirus Shows Placenta-Specific Expression and Is Upregulated in Diffuse Large B-Cell Lymphomas.Molecular biology and evolution · 2021Article
- Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Formation of RNA Granule-Derived Capsid Assembly Intermediates Appears To Be Conserved between Human Immunodeficiency Virus Type 1 and the Nonprimate Lentivirus Feline Immunodeficiency Virus.Journal of virology · 2018Article
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- Molecular Architecture of the Retroviral Capsid.Trends in biochemical sciences · 2016Review
- Mutations of Conserved Residues in the Major Homology Region Arrest Assembling HIV-1 Gag as a Membrane-Targeted Intermediate Containing Genomic RNA and Cellular Proteins.Journal of virology · 2016Article
- Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.Biophysical journal · 2015Article
- How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Virus research · 2014Review
- A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Sequence requirements for localization and packaging of Ty3 retroelement RNA.Virus research · 2013Article
- Suppression of a morphogenic mutant in Rous sarcoma virus capsid protein by a second-site mutation: a cryoelectron tomography study.Journal of virology · 2010Article
- Two-hybrid analysis of Ty3 capsid subdomain interactions.Mobile DNA · 2010Article
- Gag proteins of Drosophila telomeric retrotransposons: collaborative targeting to chromosome ends.Genetics · 2010Article
- Origin, antiviral function and evidence for positive selection of the gammaretrovirus restriction gene Fv1 in the genus Mus.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Cooperative role of the MHR and the CA dimerization helix in the maturation of the functional retrovirus capsid.Virology · 2008Article
- Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly.Journal of virology · 2008Article
- Ty3 capsid mutations reveal early and late functions of the amino-terminal domain.Journal of virology · 2007Article
- Domain-swapped dimerization of the HIV-1 capsid C-terminal domain.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Essential domains for ribonucleoprotein complex formation required for retrotransposition of telomere-specific non-long terminal repeat retrotransposon SART1.Molecular and cellular biology · 2006Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae retroviruslike element Ty3 encodes the major structural proteins capsid (CA) and nucleocapsid in the GAG3 open reading frame. The Ty3 CA protein contains a sequence (QGX2EX5FX3LX3H, where H is a hydrophobic residue) which has not been observed in other retrotransposons but which is similar to the major homology region (MHR) described for retrovirus CA. In this study the effects of mutations in the Ty3 MHR on particle formation, processing, DNA synthesis, and transposition were examined. Each of the mutations tested resulted in severe defects in transposition, with disruption occurring prior to or at particle formation, subsequent to particle formation and prior to completion of DNA synthesis, and subsequent to DNA synthesis. Changing the Q in the motif to R had relatively little effect on particle formation but decreased transposition to about 13% of that of a wild-type element. Changing G to A or V almost completely eliminated the formation of intracellular particles, possibly by disruption of CA-CA interactions. Changes introduced at the position of E resulted in blocked processing, blocked DNA synthesis, or a block at some post-reverse transcription step, depending on the nature of the mutation introduced. These results showed that the integrity of the Ty3 MHR is required for multiple aspects of Ty3 replication involving CA. These functions are independent of extracellular budding and of infection, aspects of the retroviral life cycle which are not recapitulated in replication of the Ty3 retrotransposon.
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Registered trials
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