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.
Pubmed ID: 7637788 RIS Download
Mesh terms: Amino Acid Sequence | Cloning, Molecular | Gene Products, rev | HIV-1 | HeLa Cells | Humans | Molecular Sequence Data | Nuclear Pore Complex Proteins | Nuclear Proteins | RNA-Binding Proteins | Saccharomyces cerevisiae | Sequence Homology, Amino Acid | Zinc Fingers | rev Gene Products, Human Immunodeficiency Virus
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