Histone-modifying enzymes: encrypting an enigmatic epigenetic code.
Histone-modifying enzymes catalyze a diverse array of post-translational modifications of core and linker histones within chromatin. These modifications govern a multitude of genomic functions, particularly gene expression, and are believed to constitute an epigenetic code. Histone-modifying enzymes inscribe this code by catalyzing site-selective modifications, which are subsequently interpreted by effector proteins that recognize specific covalent marks. The substrate specificity of these enzymes is of fundamental biological importance because it underpins this epigenetic code. Recently, the structural basis of this specificity has been examined with regards to recently determined structures of GCN5 acetyltransferases and SET domain methyltransferases in complex with their cognate histone substrates.
Couture
Jean-François
JF
Department of Biological Chemistry, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0606, USA.
Trievel
Raymond C
RC
D000818:Animals; D020134:Catalytic Domain; D044127:Epigenesis, Genetic; D051548:Histone Acetyltransferases / Q000737:chemistry* / Q000378:metabolism*; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry* / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D016808:Tetrahymena thermophila / Q000201:enzymology; D000099224:p300-CBP-Associated Factor
D051548:Histone Acetyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; C496551:Esa1 protein, S cerevisiae; C120128:tGCN5 histone acetyltransferase; D000099224:p300-CBP-Associated Factor