ContentsIntroductionHistonesHistones are a family of basic, positively charged proteins that associate with DNA inside the nucleus to help condense the DNA into chromatin [1]. The nuclear DNA is wrapped around the histone in order to fit in the nucleus. Nucleosomes are chromatin beads made up of DNA wrapped around eight histone proteins, or a histone octamer [1]. Four different examples of modifying histones including Histone acetylation, Histone deacetylation, Histone methylation and Histone demethylation [1]. Histone Deacetylases (HDACs)ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells [2]. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis: •Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3 •Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 •Class III - Sirtuin deacetylases •Class IV - HDAC 11 [2]. HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation [2]. HDAC8
StructureGeneral Structure InformationInhibitorPotassium Binding SiteDeacetylationZn2+ Metal Ion Mechanism Active SiteDisease
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This page was last modified 17:52, 6 April 2019.