A human nucleoporin-like protein that specifically interacts with HIV Rev
- 1 August 1995
- journal article
- Published by Springer Nature in Nature
- Vol. 376 (6540) , 530-533
- https://doi.org/10.1038/376530a0
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.Keywords
This publication has 22 references indexed in Scilit:
- A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes.The Journal of cell biology, 1995
- RNA ExportCell, 1995
- The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complexCell, 1995
- Localization of pre-mRNA splicing in mammalian nucleiNature, 1994
- Pores for thought: nuclear pore complex proteinsTrends in Cell Biology, 1994
- Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2Cell, 1993
- A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasmCell, 1993
- Functional dissection of the HIV-1 Rev trans-activator—Derivation of a trans-dominant repressor of Rev functionCell, 1989
- A novel genetic system to detect protein–protein interactionsNature, 1989
- Identification and characterization of a nuclear pore complex proteinCell, 1986