Abstract
Nucleolar shuttle protein B23 was found to bind to human immunodeficiency virus protein Tat, and this binding required the nucleolar localization motif of Tat. A fusion protein containing the B23 binding domain and beta-galactosidase caused mislocalization of Tat to the cytoplasm and inhibited the transactivation activity of Tat. These data suggest that B23 is a human factor necessary for the nucleolar localization of Tat.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Cell Nucleolus / metabolism*
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Gene Products, tat / antagonists & inhibitors
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Gene Products, tat / metabolism*
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HIV / chemistry*
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HeLa Cells
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Humans
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Nuclear Proteins / physiology*
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Nucleophosmin
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Recombinant Fusion Proteins / pharmacology
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beta-Galactosidase / pharmacology
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tat Gene Products, Human Immunodeficiency Virus
Substances
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Gene Products, tat
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Nuclear Proteins
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Recombinant Fusion Proteins
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tat Gene Products, Human Immunodeficiency Virus
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Nucleophosmin
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beta-Galactosidase