title: Dynamics of histone lysine methylation: structures of methyl writers and erasers.
abstract: In Eukarya, the packaging of DNA into chromatin provides a barrier that allows for regulation of access to the genome. Chromatin is refractory to processes acting on DNA. ATP-dependent chromatin remodeling machines and histone-modifying complexes can overcome this barrier (or strengthen it in silencing processes). Both components of chromatin (DNA and histones) are subject to postsynthetic covalent modifications, including methylation of lysines (the focus of this chapter). These lysine marks are generated by a host of histone lysine methyltransferases (writers) and can be removed by histone lysine demethylases (erasers). Importantly, epigenetic modifications impact chromatin structure directly or can be read by effector regulatory modules. Here, we summarize current knowledge on structural and functional properties of various histone lysine methyltransfereases and demethylases, with emphasis on their importance as druggable targets.
authors.affiliation: Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA.
authors.forename: Anup K
authors.initials: AK
authors.lastname: Upadhyay
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000818:Animals; D056466:Histone Demethylases / Q000737:chemistry* / Q000378:metabolism; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D006657:Histones; D056466:Histone Demethylases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine