Enzyme for Delta Antigen Acetylation

Histone acetyltransferases (HATs) modify a wide spectrum of cellular factors, including histones, coactivators, nuclear transport proteins, structural proteins, cell cycle components, transcription factors, and nuclear receptors (for reviews see Fu et al. 2004; Quivy and Van Lint 2004; and references therein). A-type HATs, which are generally localized in the nucleus and are thereby linked with transcriptional regulation, are divided into five families, including Gcn5-related acetyltranferases (GNATs), the MYST-related HATs, p300/CBP HATs, TAFII250, and nuclear hormone-related HATs (Carrozza et al. 2003). We demonstrated that S-HDAg could be acetylated in vitro by p300 (Mu et al. 2004). However, it is still possible that other acetyltransferases also participate in catalyzing S-HDAg acetylation in vivo. The cellular deacetylases (HDACs) responsible for the deacetylation of acetylated HDAg are currently under investigation.

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