ArticleNucleic acids research1992
Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein.
Article in Nucleic acids research, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 119 citations in OpenAlex.
- Deciphering hydration patterns across RNA conformations: Insights into water-mediated RNA recognition.Current research in structural biology · 2026Article
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- Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis.Current HIV research · 2020Article
- Dynamic ensemble of HIV-1 RRE stem IIB reveals non-native conformations that disrupt the Rev-binding site.Nucleic acids research · 2019Article
- Nucleolar Localization of HIV-1 Rev Is Required, Yet Insufficient for Production of Infectious Viral Particles.AIDS research and human retroviruses · 2018Article
- Contributions of Individual Domains to Function of the HIV-1 Rev Response Element.Journal of virology · 2017Article
- Probing the Structures of Viral RNA Regulatory Elements with SHAPE and Related Methodologies.Frontiers in microbiology · 2017Review
- The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.Structure (London, England : 1993) · 2016Article
- Article
- Review
- The HIV-1 Rev response element (RRE) adopts alternative conformations that promote different rates of virus replication.Nucleic acids research · 2015Article
- In vitro and in vivo analysis of the interaction between RNA helicase A and HIV-1 RNA.Journal of virology · 2012Article
- Single-nucleotide changes in the HIV Rev-response element mediate resistance to compounds that inhibit Rev function.Journal of virology · 2011Article
- Specificity of RSG-1.2 peptide binding to RRE-IIB RNA element of HIV-1 over Rev peptide is mainly enthalpic in origin.PloS one · 2011Article
- LC3-mediated fibronectin mRNA translation induces fibrosarcoma growth by increasing connective tissue growth factor.Journal of cell science · 2009Article
- Identification of the Rem-responsive element of mouse mammary tumor virus.Nucleic acids research · 2008Article
- A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA.Molecular cell · 2008Article
- Article
- Translational control of retroviruses.Nature reviews. Microbiology · 2007Review
- Targeting the A site RNA of the Escherichia coli ribosomal 30 S subunit by 2'-O-methyl oligoribonucleotides: a quantitative equilibrium dialysis binding assay and differential effects of aminoglycoside antibiotics.The Biochemical journal · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Human Immunodeficiency Virus type-1 rev protein binds with high affinity to a bubble structure located within the rev-response element (RRE) RNA in stemloop II. After this initial interaction, additional rev molecules bind to the RRE RNA in an ordered assembly process which requires a functional bubble structure, since mutations in the bubble sequence that reduce rev affinity block multiple complex formation. We have used synthetic chemistry to characterize the interaction between rev protein and its high affinity binding site. A minimal synthetic duplex RNA (RBC6) carrying the bubble and 12 flanking base pairs is able to bind rev with 1 to 1 stoichiometry and with high affinity. When the bubble structure is inserted into synthetic RNA molecules carrying longer stretches of flanking double-stranded RNA, rev forms additional complexes resembling the multimers observed with the RRE RNA. The ability of rev to bind to RBC6 analogues containing functional group modifications on base and sugar moieties of nucleoside residues was also examined. The results provide strong evidence that the bubble structure contains specific configurations of non-Watson--Crick G:G and G:A base pairs and suggest that high affinity recognition of RRE RNA by rev requires hydrogen bonding to functional groups in the major groove of a distorted RNA structure.
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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.