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Description
Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common post-transcriptional modification of Lysine involves acetylation (1). The conserved amino-terminal domains of the four core histones (H2A, H2B, H3 and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (2). Protein posttranslational reversible lysine Nε-acetylation and deacetylation have been recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progression, apoptosis, DNA repair, and cytoskeletal organization (3). The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases (4), and HDACs have become promising targets for anti-cancer drugs currently in development (5).