URACIL DNA GLYCOSYLASE SPECIFICALLY INTERACTS WITH VPR OF BOTH HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 AND SIMIAN IMMUNODEFICIENCY VIRUS OF SOOTY MANGABEYS, BUT BINDING DOES NOT CORRELATE WITH CELL-CYCLE ARREST
L. Selig et al., URACIL DNA GLYCOSYLASE SPECIFICALLY INTERACTS WITH VPR OF BOTH HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 AND SIMIAN IMMUNODEFICIENCY VIRUS OF SOOTY MANGABEYS, BUT BINDING DOES NOT CORRELATE WITH CELL-CYCLE ARREST, Journal of virology, 71(6), 1997, pp. 4842-4846
The Vpr protein encoded by human immunodeficiency virus type 1 (HIV-1)
is important for growth of virus in macrophages and prevents infected
cells from passing into mitosis (G(2) arrest). The cellular target fo
r these functions is not known, but Vpr of HIV-1 and the related Vpr f
rom simian immunodeficiency virus of sooty mangabeys (STVSM) bind the
DNA repair enzyme UNG, while the Vpx protein of SIVSM does not. Noneth
eless, a mutational analysis of Vpr showed that binding to UNG is neit
her necessary nor sufficient for the effect of Vpr on the cell cycle.