Abstract
Posttranslational modifications of histone proteins in chromatin play a critical role in the control of gene expression in eukaryotes. Histone deacetylases (HDACs) catalyze the deacetylation of lysine residues in the histone amino-terminal tails and are found in large multiprotein transcriptional compressor complexes. Human HDACs are grouped into three classes based on their similarity to known yeast factors. Class I HDACs are similar to the yeast transcriptional repressor yRPD3, whereas class II HDACs are related to yHDA1 and class III HDAs to ySIR2. In this review, we focus on the structure and function of class IIa HDACs. These recently discovered enzymes have been implicated as important regulators of gene expression during cell differentiation and development.
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