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PMID: 7637788 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A human nucleoporin-like protein that specifically interacts with HIV Rev.

Nature ·Vol. 376 ·No. 6540 ·1995-08-10 ·Pages 530-3

Fritz CC, Zapp ML, Green MR

Abstract

The Rev protein of human immunodeficiency virus type 1 (HIV-1) facilitates the nuclear export of unspliced and partly spliced viral RNAs. Rev contains an RNA binding domain, required for interaction with HIV-1 RNA, and an effector domain, required for RNA-bound Rev to function. The Rev effector domain is believed to interact with a cellular cofactor required for the Rev response and thus HIV-1 replication. Here we report the use of a yeast two-hybrid screen to clone human Rev interacting protein (hRIP), which specifically interacts with the Rev effector domain. This hRIP protein has homology with nucleoporins, a class of proteins that mediate nucleocytoplasmic transport. These and other properties of hRIP are those expected of a Rev cellular cofactor.

MeSH Terms
Amino Acid Sequence Cloning, Molecular Gene Products, rev/metabolism HIV-1/metabolism HeLa Cells Humans Molecular Sequence Data Nuclear Pore Complex Proteins Nuclear Proteins/genetics,metabolism RNA-Binding Proteins Saccharomyces cerevisiae/metabolism Sequence Homology, Amino Acid Zinc Fingers/genetics rev Gene Products, Human Immunodeficiency Virus
Chemicals
AGFG1 protein, human Gene Products, rev Nuclear Pore Complex Proteins Nuclear Proteins RNA-Binding Proteins rev Gene Products, Human Immunodeficiency Virus
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fritz C C
Howard Hughes Medical Institute, Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605, USA.
Zapp M L
Green M R
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-08-10
Pages
530-3
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
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