Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants

Chaitanya Jain, Joel G. Belasco

Research output: Contribution to journalArticle

73 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)603-614
Number of pages12
JournalMolecular Cell
Volume7
Issue number3
DOIs
StatePublished - Mar 1 2001
Externally publishedYes

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Structural Models
HIV-1
RNA
Proteins
Electrophoretic Mobility Shift Assay
Head
Escherichia coli

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. / Jain, Chaitanya; Belasco, Joel G.

In: Molecular Cell, Vol. 7, No. 3, 01.03.2001, p. 603-614.

Research output: Contribution to journalArticle

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