HIV-1反式激活蛋白在体外发生多聚（ADP-核糖）化。

HIV-1 Tat protein is poly(ADP-ribosyl)ated in vitro.

作者信息

Kameoka M, Tanaka Y, Ota K, Itaya A, Yamamoto K, Yoshihara K

机构信息

Department of Biochemistry, Nara Medical University, Nara, Kashihara, 634-8521, Japan.

出版信息

Biochem Biophys Res Commun. 1999 Jul 22;261(1):90-4. doi: 10.1006/bbrc.1999.0964.

DOI:10.1006/bbrc.1999.0964

PMID:10405328

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.

摘要

纯化的重组HIV-1 Tat蛋白以剂量依赖的方式刺激了聚（ADP-核糖）聚合酶的受体依赖性反应。通过SDS-聚丙烯酰胺凝胶电泳分析反应产物，随后用抗聚（ADP-核糖）抗体进行免疫印迹，结果显示重组Tat蛋白在酶反应中被聚（ADP-核糖）共价修饰。尽管在Tat与TAR（病毒反式激活应答元件）RNA形成特异性复合物的活性中未检测到这种修饰的显著影响，但目前的结果增加了聚（ADP-核糖）聚合酶通过修饰病毒编码的反式激活因子Tat蛋白参与HIV-1调节的可能性。