title: Structure and function of histone acetyltransferases.
abstract: Histone acetyltranferase (HAT) enzymes are the catalytic subunit of large multisubunit HAT complexes that acetylate the epsilon-amino group of specific lysine residues on histone tails to promote transcriptional activation. Recent structural and functional studies on the divergent HAT enzymes Gcn5/PCAF, Esa1 and Hat1 have provided new insights into the underlying mechanism of histone binding and acetylation by HAT proteins. The three HAT enzymes contain a structurally conserved core domain that plays a functionally conserved role in binding the coenzyme A cofactor and in harboring the putative general base for catalysis. Structurally variable N- and C-terminal domains appear to contain a related scaffold that mediates histone substrate binding. These data provide a framework for understanding the structure and function of other more divergent HAT proteins such as TAF(II)250 and CBP/p300, and provides a starting point for understanding how HAT proteins may cooperate with other factors within in vivo HAT complexes to promote transcriptional activation.
authors: The Wistar Institute and the Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA. marmor@wistar.upenn.edu
authors: R
authors: R
authors: Marmorstein
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D003065:Coenzyme A / Q000378:metabolism; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D005810:Multigene Family; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014158:Transcription, Genetic
chemical_list: D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D003065:Coenzyme A