A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element.
The constitutive transport element (CTE) of type D retroviruses mediates the nuclear export of unspliced viral transcripts. We previously showed that RNA helicase A functionally interacts with CTE and contains a bidirectional nuclear transport domain at the carboxyl terminus. Here we report the identification of a novel human protein, helicase ... A-binding protein 95 (HAP95), which specifically binds to the carboxyl terminus of RNA helicase A. HAP95 is partially homologous to AKAP95, a member of the A kinase-anchoring protein family, but lacks the protein kinase A binding domain characteristic of this family. HAP95 is a nuclear protein at steady state but shuttles between the nucleus and cytoplasm. Overexpression of HAP95 significantly increases CTE-dependent gene expression but has no effect on general gene expression or that mediated by the Rev/Rev response element of human immunodeficiency virus type 1.
Mesh Terms:
Amino Acid Sequence, Autoantigens, Base Sequence, Betaretrovirus, Carrier Proteins, DEAD-box RNA Helicases, DNA-Binding Proteins, Female, Gene Library, Hela Cells, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Neoplasm Proteins, Nuclear Proteins, Placenta, Pregnancy, RNA Helicases, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, T-Lymphocytes, Transfection
Amino Acid Sequence, Autoantigens, Base Sequence, Betaretrovirus, Carrier Proteins, DEAD-box RNA Helicases, DNA-Binding Proteins, Female, Gene Library, Hela Cells, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Neoplasm Proteins, Nuclear Proteins, Placenta, Pregnancy, RNA Helicases, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, T-Lymphocytes, Transfection
J. Biol. Chem.
Date: Jul. 14, 2000
PubMed ID: 10748171
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