       Document 0652
 DOCN  M9640652
 TI    Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA
       glycosylase DNA repair enzyme.
 DT    9604
 AU    Bouhamdan M; Benichou S; Rey F; Navarro JM; Agostini I; Spire B; Camonis
       J; Slupphaug G; Vigne R; Benarous R; Sire J; INSERM U372, 13276
       Marseille, France.
 SO    J Virol. 1996 Feb;70(2):697-704. Unique Identifier : AIDSLINE
       MED/96135176
 AB    The role of the accessory gene product Vpr during human immunodeficiency
       virus type 1 infection remains unclear. We have used the yeast
       two-hybrid system to identify cellular proteins that interact with Vpr
       and could be involved in its function. A cDNA clone which encodes the
       human uracil DNA glycosylase (UNG), a DNA repair enzyme involved in
       removal of uracil in DNA, has been isolated. Interaction between Vpr and
       UNG has been demonstrated by in vitro protein-protein binding assays
       using translated, radiolabeled Vpr and UNG recombinant proteins
       expressed as a glutathione S-transferase fusion protein. Conversely,
       purified UNG has been demonstrated to interact with Vpr recombinant
       protein expressed as a glutathione S-transferase fusion protein.
       Coimmunoprecipitation experiments confirmed that Vpr and UNG are
       associated within cells expressing Vpr. By using a panel of C- and
       N-terminally deleted Vpr mutants, we have determined that the core
       protein of Vpr, spanning amino acids 15 to 77, is involved in the
       interaction with UNG. We also demonstrate by in vitro experiments that
       the enzymatic activity of UNG is retained upon interaction with Vpr.
 DE    Animal  Base Sequence  Binding Sites  DNA Primers  *DNA Repair  Gene
       Products, vpr/CHEMISTRY/GENETICS/*METABOLISM  Glutathione
       Transferases/GENETICS/METABOLISM  Hela Cells  Human  HIV-1/*METABOLISM
       Molecular Sequence Data  Nucleosidases/GENETICS/*METABOLISM  Precipitin
       Tests  Recombinant Fusion Proteins/CHEMISTRY/GENETICS/METABOLISM
       Support, Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

