Journal article

Acetylated tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32

R Berro, K Kehn, C de la Fuente, A Pumfery, R Adair, J Wade, AM Colberg-Poley, J Hiscott, F Kashanchi

Journal of Virology | AMER SOC MICROBIOLOGY | Published : 2006

Abstract

The human immunodeficiency virus type 1 (HIV-1) potent transactivator Tat protein mediates pleiotropic effects on various cell functions. Posttranslational modification of Tat affects its activity during viral transcription. Tat binds to TAR and subsequently becomes acetylated on lysine residues by histone acetyltransferases. Novel protein-protein interaction domains on acetylated Tat are then established, which are necessary for both sustained transcriptional activation of the HIV-1 promoter and viral transcription elongation. In this study, we investigated the identity of proteins that preferentially bound acetylated Tat. Using a proteomic approach, we identified a number of proteins that ..

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