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Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region.

J Virol

April 2007

McGill University AIDS Centre, Department of Medicine, Terry Fox Molecular Oncology Group, Lady Davis Institute, St. Mortimer B. Davis Jewish General Hospital, 3755 Côte-Ste-Catherine Rd., Montréal, Québec H3T 1E2, Canada.

Arginine methylation has been shown to regulate signal transduction, protein subcellular localization, gene transcription, and protein-protein interactions that ultimately alter gene expression. Although the role of cellular protein arginine methyltransferases (PRMT) in viral gene expression is largely unknown, we recently showed that the Tat protein of human immunodeficiency virus type 1 (HIV-1) is a substrate for one such enzyme, termed PRMT6. However, the mechanism by which arginine methylation impairs the transactivation potential of Tat and the sites of arginine methylation within Tat remain obscure.

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