ArticleProtein science : a publication of the Protein Society2008
Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 37 citations in OpenAlex.
- RNA splicing patterns contribute to burst size variation among HIV-1-infected Jurkat cell clones.Journal of virology · 2025Article
- Rev Protein Diversity in HIV-1 Group M Clades.Viruses · 2024Article
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- HIV-1 Rev-RRE functional activity in primary isolates is highly dependent on minimal context-dependent changes in Rev.Scientific reports · 2022Article
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- HIV-1 resists MxB inhibition of viral Rev protein.Emerging microbes & infections · 2020Article
- Native mass spectrometry reveals the initial binding events of HIV-1 rev to RRE stem II RNA.Nature communications · 2020Article
- Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis.Current HIV research · 2020Article
- A Survey of DDX21 Activity During Rev/RRE Complex Formation.Journal of molecular biology · 2018Article
- Identification of a homogenous structural basis for oligomerization by retroviral Rev-like proteins.Retrovirology · 2017Article
- A DEAD-Box Helicase Mediates an RNA Structural Transition in the HIV-1 Rev Response Element.Journal of molecular biology · 2017Article
- The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.Structure (London, England : 1993) · 2016Article
- Review
- Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding.Retrovirology · 2014Article
- Article
- Host cell interactome of HIV-1 Rev includes RNA helicases involved in multiple facets of virus production.Molecular & cellular proteomics : MCP · 2012Article
- The structure of Aquifex aeolicus ribosomal protein S8 reveals a unique subdomain that contributes to an extremely tight association with 16S rRNA.Journal of molecular biology · 2012Article
- DDX1 is an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication.Journal of molecular biology · 2012Article
- Formation of trans-activation competent HIV-1 Rev:RRE complexes requires the recruitment of multiple protein activation domains.PloS one · 2012Article
- The HIV-1 Rev response element: an RNA scaffold that directs the cooperative assembly of a homo-oligomeric ribonucleoprotein complex.RNA biology · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The translation of the unspliced and partially spliced viral mRNAs that encode the late, structural proteins of HIV-1 depends on the viral-protein Rev. Oligomeric binding of Rev to the Rev response element (RRE) in these mRNAs promotes their export from the nucleus and thus controls their expression. Here, we compared the effects of hydrophobic to hydrophilic mutations within the oligomerization domain of Rev using assays for oligomeric RNA binding, protein structure, and export from the nucleus. Oligomeric RNA binding alone does not correlate well with RNA transport activity in the subset of mutants. However, protein structure as judged by CD spectroscopy does correlate well with Rev function. The oligomeric assembly of Rev-L18T is impaired but exhibits minor defects in structure and retains a basal level of activity in vivo. The prevalence of L18T in infected individuals suggests a positive selection mechanism for L18T modulation of Rev activity that may delay the onset of AIDS.
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