Histone acetyltransferases: function, structure, and catalysis.
Histone acetyltransferases (HATs) directly link chromatin modification to gene activation. Recent structure/function studies provide insights into HAT catalysis and histone binding, and genetic studies suggest cross-talk between acetylation and other histone modifications. Developmental aberrations in mice and certain human cancers are associated with HAT mutations, further highlighting the importance of these enzymes to normal cell growth and differentiation.
Marmorstein
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Structural Biology Program, The Wistar Institute, Philadelphia, Pennsylvania 19104, USA. marmor@wistar.upenn.edu
Roth
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D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D005314:Embryonic and Fetal Development; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism*; D006801:Humans; D051379:Mice; D009369:Neoplasms / Q000209:etiology; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic; D015003:Yeasts / Q000201:enzymology
D002843:Chromatin; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases