Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation

被引:41
作者
Davis, DA
Brown, CA
Newcomb, FM
Boja, ES
Fales, HM
Kaufman, J
Stahl, SJ
Wingfield, P
Yarchoan, R
机构
[1] NCI, CCR, HIV & AIDS Malignancy Branch, NIH, Bethesda, MD 20892 USA
[2] NHLBI, Lab Biophys Chem, NIH, Bethesda, MD 20892 USA
[3] NIAMSD, Prot Express Lab, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1128/JVI.77.5.3319-3325.2003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Human immunodeficiency virus protease activity can be regulated by reversible oxidation of a sulfur-containing amino acid at the dimer interface. We show here that oxidation of this amino acid in human immunodeficiency virus type I protease prevents dimer formation. Moreover, we show that human T-cell leukemia virus type I protease can be similarly regulated through reversible glutathionylation of its two conserved cysteine residues. Based on the known three-dimensional structures and multiple sequence alignments of retroviral proteases, it is predicted that the majority of retroviral proteases have sulfur-containing amino acids at the dimer interface. The regulation of protease activity by the modification of a sulfur-containing amino acid at the dimer interface may be a conserved mechanism among the majority of retroviruses.
引用
收藏
页码:3319 / 3325
页数:7
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