ArticleJournal of virology2004
Basic residues of the retroviral nucleocapsid play different roles in gag-gag and Gag-Psi RNA interactions.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- An Infectious Rous Sarcoma Virus Gag Mutant That Is Defective in Nuclear Cycling.Journal of virology · 2021Article
- Intercellular Communication in the Nervous System Goes Viral.Trends in neurosciences · 2021Review
- Rous Sarcoma Virus Genomic RNA Dimerization Capability In Vitro Is Not a Prerequisite for Viral Infectivity.Viruses · 2020Article
- Article
- Mutations in the Basic Region of the Mason-Pfizer Monkey Virus Nucleocapsid Protein Affect Reverse Transcription, Genomic RNA Packaging, and the Virus Assembly Site.Journal of virology · 2018Article
- Orchestrating the Selection and Packaging of Genomic RNA by Retroviruses: An Ensemble of Viral and Host Factors.Viruses · 2016Review
- The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranes.Journal of virology · 2015Article
- Interplay between the alpharetroviral Gag protein and SR proteins SF2 and SC35 in the nucleus.Frontiers in microbiology · 2015Article
- The roles of lipids and nucleic acids in HIV-1 assembly.Frontiers in microbiology · 2014Review
- Virus morphogenesis in the cell: methods and observations.Sub-cellular biochemistry · 2013Review
- Beyond plasma membrane targeting: role of the MA domain of Gag in retroviral genome encapsidation.Journal of molecular biology · 2011Review
- Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.Journal of virology · 2009Article
- The C terminus of foamy retrovirus Gag contains determinants for encapsidation of Pol protein into virions.Journal of virology · 2008Article
- Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription.Journal of virology · 2008Article
- Nucleocapsid protein function in early infection processes.Virus research · 2008Review
- Ty3 nucleocapsid controls localization of particle assembly.Journal of virology · 2008Article
- Solution structure of the Rous sarcoma virus nucleocapsid protein: muPsi RNA packaging signal complex.Journal of molecular biology · 2007Article
- Redundant roles for nucleocapsid and matrix RNA-binding sequences in human immunodeficiency virus type 1 assembly.Journal of virology · 2005Article
- Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity.Journal of virology · 2005Article
- Cooperative effect of gag proteins p12 and capsid during early events of murine leukemia virus replication.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The Orthoretrovirus Gag interaction (I) domain maps to the nucleocapsid (NC) domain in the Gag polyprotein. We used the yeast two-hybrid system to analyze the role of Alpharetrovirus NC in Gag-Gag interactions and also examined the efficiency of viral assembly and release in vivo. We could delete either or both of the two Cys-His (CH) boxes without abrogating Gag-Gag interactions. We found that as few as eight clustered basic residues, attached to the C terminus of the spacer peptide separating the capsid (CA) and NC domains in the absence of NC, was sufficient for Gag-Gag interactions. Our results support the idea that a sufficient number of basic residues, rather than the CH boxes, play the important role in Gag multimerization. We also examined the requirement for basic residues in Gag for packaging of specific packaging signal (Psi)-containing RNA. Using a yeast three-hybrid RNA-protein interaction assay, second-site suppressors of a packaging-defective Gag mutant were isolated, which restored Psi RNA binding. These suppressors mapped to the p10 or CA domains in Gag and resulted in either introduction of a positively charged residue or elimination of a negatively charged one. These results imply that the structural interactions of NC with other domains of Gag are necessary for Psi RNA binding. Taken together, our results show that while Gag assembly only requires a certain number of positively charged amino acids, Gag binding to genomic RNA for packaging requires more complex interactions inherent in the protein tertiary structure.
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