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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Dose-Response Relationship, Drug
  • Gene Products, tat / biosynthesis
  • Gene Products, tat / isolation & purification
  • Gene Products, tat / metabolism*
  • HIV Long Terminal Repeat / genetics
  • HIV-1*
  • Poly Adenosine Diphosphate Ribose / metabolism*
  • Poly(ADP-ribose) Polymerases / metabolism*
  • Protein Binding
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • tat Gene Products, Human Immunodeficiency Virus

Substances

  • Gene Products, tat
  • RNA, Viral
  • Recombinant Fusion Proteins
  • tat Gene Products, Human Immunodeficiency Virus
  • Poly Adenosine Diphosphate Ribose
  • Poly(ADP-ribose) Polymerases