Acetylation of internal lysine residues of core histone N-terminal domains has been found correlatively associated with transcriptional activation in eukaryotes for more than three decades. Recent discoveries showing that several transcriptional regulators possess intrinsic histone acetyltransferase
Regulation of histone deacetylase activities
โ Scribed by Nilanjan Sengupta; Edward Seto
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 141 KB
- Volume
- 93
- Category
- Article
- ISSN
- 0730-2312
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โฆ Synopsis
Abstract
Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl groups from lysine residues in both histone and nonโhistone proteins. They play a key role in the regulation of gene transcription and many other biological processes involving chromatin. Significantly, recent studies suggest that HDACs are critically involved in cellโcycle regulation, cell proliferation, differentiation, and in the development of human cancer. HDAC inhibitors currently are being exploited as potential antiโcancer agents. As expected for vital regulators of many cellular processes, the activities of HDACs are tightly controlled and precisely regulated by multiple mechanisms. The activities of most if not all HDACs are regulated by proteinโprotein interactions. In addition, many HDACs are regulated by postโtranslational modifications as well as by subcellular localization. Less studied, but perhaps equally important, is the regulation of some HDACs by control of expression, availability of cofactors, and by proteolytic processing. A complete understanding of how HDACs are regulated will contribute not only to our overall knowledge of chromatin structure and gene control, but will offer tremendous insight into approaches for developing therapeutic HDAC inhibitors with improved specificity. ยฉ 2004 WileyโLiss, Inc.
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