Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: A dual function for an arginine-rich binding motif

Maria L. Zapp*, Thomas J. Hope, Tristram G. Parslow, Michael R. Green

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

200 Scopus citations

Abstract

The Rev protein of human immunodeficiency virus type 1 is a sequence-specific RNA binding protein that is essential for viral replication. Here we present evidence that Rev is a stable oligomer both in vitro and in vivo. Analysis of Rev mutants indicates that oligomerization is essential for RNA binding and hence Rev function. The oligomerization and RNA binding domains overlap over 47 amino acids. Within this region is a short arginine-rich motif found in a large class of RNA binding proteins. Substitution of multiple residues within the arginine-rich motif abolishes oligomerization, whereas several single-amino-acid substitution mutants oligomerize but do not bind RNA. Thus, Rev's arginine-rich motif participates in two distinct functions: oligomerization and RNA binding.

Original languageEnglish (US)
Pages (from-to)7734-7738
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number17
DOIs
StatePublished - 1991

Keywords

  • MRNA export
  • Pre-mRNA splicing
  • RNA binding protein
  • Virus expression

ASJC Scopus subject areas

  • General

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