Abstract
Purified recombinant HIV-1 Tat protein stimulated acceptor-dependent reaction of poly(ADP-ribose) polymerase in a dose-dependent manner. Analysis of the reaction products by SDS-polyacrylamide gel electrophoresis followed by immunoblotting with anti-poly(ADP-ribose) antibody revealed that recombinant Tat proteins were covalently modified with poly(ADP-ribose) in the enzyme reaction. Eventhough no significant effect of the modification was detected in the activity of Tat to form a specific complex with TAR (a viral transactivation response element) RNA, the present results raise the possibility that poly(ADP-ribose) polymerase is involved in the regulation of HIV-1 through the modification of a virus-encoded transactivator, Tat protein.
Copyright 1999 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blotting, Western
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Dose-Response Relationship, Drug
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Gene Products, tat / biosynthesis
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Gene Products, tat / isolation & purification
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Gene Products, tat / metabolism*
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HIV Long Terminal Repeat / genetics
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HIV-1*
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Poly Adenosine Diphosphate Ribose / metabolism*
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Poly(ADP-ribose) Polymerases / metabolism*
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Protein Binding
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RNA, Viral / genetics
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RNA, Viral / metabolism
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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tat Gene Products, Human Immunodeficiency Virus
Substances
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Gene Products, tat
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RNA, Viral
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Recombinant Fusion Proteins
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tat Gene Products, Human Immunodeficiency Virus
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Poly Adenosine Diphosphate Ribose
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Poly(ADP-ribose) Polymerases