Erasers of Histone Acetylation: The Histone Deacetylase Enzymes
Author(s) -
Ed Seto,
Minoru Yoshida
Publication year - 2014
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a018713
Subject(s) - acetylation , histone , biology , histone deacetylase , histone deacetylase 2 , chromatin , histone acetyltransferases , biochemistry , hdac11 , epigenetics , enzyme , histone deacetylase 5 , histone modifying enzymes , lysine , microbiology and biotechnology , histone methyltransferase , dna , amino acid , gene
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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