Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif
UMass Chan Affiliations
Program in Molecular MedicineDocument Type
Journal ArticlePublication Date
1991-09-01Keywords
Amino Acid SequenceAnimals
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
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7734-8.