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

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  • 1. Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.
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    • Zapp ML 1
    (1 author)

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Proceedings of the National Academy of Sciences of the United States of America, 01 Sep 1991, 88(17):7734-7738
https://doi.org/10.1073/pnas.88.17.7734 PMID: 1715576 PMCID: PMC52377

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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.

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Proc Natl Acad Sci U S A. 1991 Sep 1; 88(17): 7734–7738.
PMCID: PMC52377
PMID: 1715576

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

M L Zapp, T J Hope, T G Parslow, and M R Green
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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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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