ArticleJournal of virology2003
Importance of basic residues in binding of rous sarcoma virus nucleocapsid to the RNA packaging signal.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- An Infectious Rous Sarcoma Virus Gag Mutant That Is Defective in Nuclear Cycling.Journal of virology · 2021Article
- 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
- 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
- Beyond plasma membrane targeting: role of the MA domain of Gag in retroviral genome encapsidation.Journal of molecular biology · 2011Review
- Genetic evidence for a connection between Rous sarcoma virus gag nuclear trafficking and genomic RNA packaging.Journal of virology · 2009Article
- The C terminus of foamy retrovirus Gag contains determinants for encapsidation of Pol protein into virions.Journal of virology · 2008Article
- 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
- 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
- Exposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173).Journal of virology · 2005Article
- Role of the C terminus of foamy virus Gag in RNA packaging and Pol expression.Journal of virology · 2004Article
- Basic residues of the retroviral nucleocapsid play different roles in gag-gag and Gag-Psi RNA interactions.Journal of virology · 2004Article
- RNA sequences in the Moloney murine leukemia virus genome bound by the Gag precursor protein in the yeast three-hybrid system.Journal of virology · 2004Article
- Involvement of the matrix and nucleocapsid domains of the bovine leukemia virus Gag polyprotein precursor in viral RNA packaging.Journal of virology · 2003Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In the context of the Rous sarcoma virus Gag polyprotein, only the nucleocapsid (NC) domain is required to mediate the specificity of genomic RNA packaging. We have previously showed that the Saccharomyces cerevisiae three-hybrid system provides a rapid genetic assay to analyze the RNA and protein components of the avian retroviral RNA-Gag interactions necessary for specific encapsidation. In this study, using both site-directed mutagenesis and in vivo random screening in the yeast three-hybrid binding assay, we have examined the amino acids in NC required for genomic RNA binding. We found that we could delete either of the two Cys-His boxes without greatly abrogating either RNA binding or packaging, although the two Cys-His boxes are likely to be required for efficient viral assembly and release. In contrast, substitutions for the Zn-coordinating residues within the boxes did prevent RNA binding, suggesting changes in the overall conformation of the protein. In the basic region between the two Cys-His boxes, three positively charged residues, as well as basic residues flanking the two boxes, were necessary for both binding and packaging. Our results suggest that the stretches of positively charged residues within NC that need to be in a proper conformation appear to be responsible for selective recognition and binding to the packaging signal (Psi)-containing RNAs.
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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.