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PMID: 1715576 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 17 ·1991-09-01 ·Pages 7734-8

Zapp ML, Hope TJ, Parslow TG, Green MR

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.

MeSH Terms
Amino Acid Sequence Animals Arginine Binding Sites Cell Line Cloning, Molecular Escherichia coli/genetics Gene Products, rev/genetics,isolation & purification,metabolism Genes, rev HIV-1/genetics,metabolism Macromolecular Substances Molecular Sequence Data Molecular Weight RNA/metabolism Recombinant Proteins/isolation & purification,metabolism Transcription, Genetic rev Gene Products, Human Immunodeficiency Virus
Chemicals
Gene Products, rev Macromolecular Substances Recombinant Proteins rev Gene Products, Human Immunodeficiency Virus RNA Arginine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Zapp M L
Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.
Hope T J
Parslow T G
Green M R
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29 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.17.7734
Published
1991-09-01
Pages
7734-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC52377
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.88.17.7734 PMC Full Text View journal details
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