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. 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）. Protein post-translational 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. The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases，and HDACs have become promising targets for anti-cancer drugs currently in development.
