Structural Model for the Cooperative Assembly of HIV-1 Rev Multimers on the RRE as Deduced from Analysis of Assembly-Defective Mutants
Identifieur interne : 000A05 ( Istex/Curation ); précédent : 000A04; suivant : 000A06Structural Model for the Cooperative Assembly of HIV-1 Rev Multimers on the RRE as Deduced from Analysis of Assembly-Defective Mutants
Auteurs : Chaitanya Jain [États-Unis] ; Joel G. Belasco [États-Unis]Source :
- Molecular Cell [ 1097-2765 ] ; 2001.
English descriptors
- Teeft :
- Amino, Amino acid residues, Amino acid side chains, Amino acid substitutions, Amino acids, Belasco, Binding affinity, Binding domain, Binding domains, Binding site, Binding sites, Biochemical screening, Biol, Coli, Coli extracts, Coli strain, Colony color, Cooperative assembly, Cooperative interactions, Cullen, Dimer, Dimeric, Dimeric complexes, Dissociation constants, Electrophoretic mobility, Encoding, Escherichia coli, Galactosidase, Galactosidase activity, Head residues, Head surface, Helix, Human immunodeficiency virus type, Hydrophobic, Immunodeficiency, Intramolecular interface, Intrinsic affinity, Jain, Lacz, Malim, Methods enzymol, Molecular cell, Molecule, Monomer, Monomeric, Mrna, Multimer, Multimeric, Multimeric assembly, Multimerization, Multimerization mutants, Multimers, Mutant, Mutation, Nucleating, Nucleating molecule, Phenotype, Plasmid, Plasmid library, Point mutation, Prev1, Protein concentration, Protein concentrations, Protein interactions, Protein residues, Radiolabeled, Reporter mrna, Repression ratio, Repression ratios, Residue, Retardation analysis, Secondary structure, Side chains, Single copy, Structural model, Substitution, Tail residues, Tail surface, Transformants, Translational, Translational repression, Trimeric complexes, Variant, Various complexes.
Abstract
Abstract: The functional efficacy of the HIV-1 Rev protein is highly dependent on its ability to assemble onto its HIV-1 RNA target (the RRE) as a multimeric complex. To elucidate the mechanism of multimeric assembly, we have devised two rapid and broadly applicable strategies for examining cooperative interactions between proteins bound to RNA, one based on cooperative translational repression of a two-site reporter and the other on gel shift analysis with crude E. coli extracts. Using these strategies, we have identified two distinct surfaces of Rev (head and tail) that are critical for different steps in multimeric assembly. Our data indicate that Rev assembles cooperatively on the RRE via a series of symmetrical tail-to-tail and head-to-head protein–protein interactions. The insights into molecular architecture suggested by these findings have enabled us to derive a structural model for Rev and its multimerization on the RRE.
Url:
DOI: 10.1016/S1097-2765(01)00207-6
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<term>Amino acids</term>
<term>Belasco</term>
<term>Binding affinity</term>
<term>Binding domain</term>
<term>Binding domains</term>
<term>Binding site</term>
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<term>Biol</term>
<term>Coli</term>
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<term>Cooperative interactions</term>
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<term>Dimer</term>
<term>Dimeric</term>
<term>Dimeric complexes</term>
<term>Dissociation constants</term>
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<term>Galactosidase</term>
<term>Galactosidase activity</term>
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<term>Multimers</term>
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<term>Mutation</term>
<term>Nucleating</term>
<term>Nucleating molecule</term>
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<term>Plasmid library</term>
<term>Point mutation</term>
<term>Prev1</term>
<term>Protein concentration</term>
<term>Protein concentrations</term>
<term>Protein interactions</term>
<term>Protein residues</term>
<term>Radiolabeled</term>
<term>Reporter mrna</term>
<term>Repression ratio</term>
<term>Repression ratios</term>
<term>Residue</term>
<term>Retardation analysis</term>
<term>Secondary structure</term>
<term>Side chains</term>
<term>Single copy</term>
<term>Structural model</term>
<term>Substitution</term>
<term>Tail residues</term>
<term>Tail surface</term>
<term>Transformants</term>
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<term>Translational repression</term>
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<front><div type="abstract" xml:lang="en">Abstract: The functional efficacy of the HIV-1 Rev protein is highly dependent on its ability to assemble onto its HIV-1 RNA target (the RRE) as a multimeric complex. To elucidate the mechanism of multimeric assembly, we have devised two rapid and broadly applicable strategies for examining cooperative interactions between proteins bound to RNA, one based on cooperative translational repression of a two-site reporter and the other on gel shift analysis with crude E. coli extracts. Using these strategies, we have identified two distinct surfaces of Rev (head and tail) that are critical for different steps in multimeric assembly. Our data indicate that Rev assembles cooperatively on the RRE via a series of symmetrical tail-to-tail and head-to-head protein–protein interactions. The insights into molecular architecture suggested by these findings have enabled us to derive a structural model for Rev and its multimerization on the RRE.</div>
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