Title

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

UMMS Affiliation

Program in Molecular Medicine

Publication Date

9-1-1991

Document Type

Article

Subjects

Amino Acid Sequence; Animals; Arginine; Binding Sites; Cell Line; Cloning, Molecular; Escherichia coli; Gene Products, rev; *Genes, rev; HIV-1; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; RNA; Recombinant Proteins; Transcription, Genetic; rev Gene Products, Human Immunodeficiency Virus

Disciplines

Life Sciences | Medicine and Health Sciences

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.

Rights and Permissions

Citation: Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7734-8.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Proceedings of the National Academy of Sciences of the United States of America

PubMed ID

1715576