Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif
Program in Molecular Medicine
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
Life Sciences | Medicine and Health Sciences
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.
Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7734-8.
Proceedings of the National Academy of Sciences of the United States of America
Zapp, Maria L.; Hope, Thomas J.; Parslow, Tristram G.; and Green, Michael R., "Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif" (1991). Open Access Articles. 1825.