A structural model for the HIV-1 Rev-RRE complex deduced from altered- specificity Rev variants isolated by a rapid genetic strategy

Chaitanya Jain, Joel G. Belasco

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

A broadly applicable genetic strategy was developed for investigating RNA-protein interactions and applied to the HIV-1 Ray protein. By rapidly screening thousands of Rev-RNA interactions in Escherichia coli, we isolated Rev suppressor mutations that alleviated the deleterious effect of mutations in RRE stem-loop IIB, the high affinity RNA-binding site for Rev. All of these suppressor mutations map to a single arginine-deficient face of a Rev α-helix, and some alter the binding specificity of the protein, providing genetic evidence for direct contacts between specific Rev amino acids and RNA nucleotides in the RNA complex of Rev. The spatial constraints suggested by these data have enabled us to model the structure of this complex.

Original languageEnglish
Pages (from-to)115-125
Number of pages11
JournalCell
Volume87
Issue number1
DOIs
StatePublished - Oct 1 1996
Externally publishedYes

Fingerprint

Structural Models
HIV-1
RNA
Genetic Suppression
Proteins
Escherichia coli
Arginine
Carrier Proteins
Screening
Nucleotides
Binding Sites
Amino Acids
Mutation

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

A structural model for the HIV-1 Rev-RRE complex deduced from altered- specificity Rev variants isolated by a rapid genetic strategy. / Jain, Chaitanya; Belasco, Joel G.

In: Cell, Vol. 87, No. 1, 01.10.1996, p. 115-125.

Research output: Contribution to journalArticle

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