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M9640652.TXT
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1996-03-04
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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).