Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6.

Reversible acetylation of Tat is critical for its transactivation activity toward HIV-1 transcription. However, the enzymes involved in the acetylation/deacetylation cycles have not been fully characterized. In this study, by yeast two-hybrid assay, we have discovered the histone deacetylase HDAC6 to be a binding partner of Tat. Our data show ...
that HDAC6 interacts with Tat in the cytoplasm in a microtubule-dependent manner. In addition, HDAC6 deacetylates Tat at Lys-28 and thereby suppresses Tat-mediated transactivation of the HIV-1 promoter. Inactivation of HDAC6 promotes the interaction of Tat with cyclin T1 and leads to an increase in Tat transactivation activity. These findings establish HDAC6 as a Tat deacetylase and support a model in which Lys-28 deacetylation decreases Tat transactivation activity through affecting the ability of Tat to form a ribonucleoprotein complex with cyclin T1 and the transactivation-responsive RNA.
Mesh Terms:
Acetylation, Animals, Cyclin T, Gene Expression Regulation, Viral, HEK293 Cells, HIV-1, Histone Deacetylases, Humans, Jurkat Cells, Mice, Mice, Knockout, Microtubules, Promoter Regions, Genetic, Transcription, Genetic, Transcriptional Activation, tat Gene Products, Human Immunodeficiency Virus
J. Biol. Chem.
Date: Mar. 18, 2011
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