Erasers of Histone Acetylation: The Histone Deacetylase Enzymes
- 1Department of Molecular Oncology, Moffitt Cancer Center and Research Institute, Tampa, Florida 33612
- 2Chemical Genetics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
- Correspondence: ed.seto{at}moffitt.org
Abstract
Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD+-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.
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