HIV-1 Tat protein is poly(ADP-ribosyl)ated in vitro. |
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| Authors: | M Kameoka Y Tanaka K Ota A Itaya K Yamamoto K Yoshihara |
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| Affiliation: | Department of Biochemistry, Nara Medical University, Nara, Kashihara, 634-8521, Japan. |
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| 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. |
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