组蛋白乙酰化-去乙酰化-综述.pdf

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Chembiochem. Author manuscript; available in PMC 2012 April 17.
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Chembiochem. 2011 January 24; 12(2): 290–298. doi:.
KAT(ching) Metabolism by the Tail: Insight into the links
between lysine acetyltransferases and metabolism
Brittany N. Albaugh**,[a], Kevin M. Arnold**,[a], and Prof. Dr. John M Denu*,[a]
[a]Department of Biomolecular Chemistry, School of Medicine and Public Health, University of
Wisconsin, 1300 University Ave., Madison, WI 53706, Fax:
Abstract
Post-translational modifications of histones elicit structural and functional changes within
chromatin that regulate various epigenetic processes. Epigenetic mechanisms rely on enzymes
whose activities are driven by co-enzymes and metabolites from intermediary metabolism. Lysine
acetyltransferases (KATs) catalyze the transfer of acetyl groups from acetyl-CoA to epsilon amine
groups. Utilization of this critical metabolite suggests these enzymes are modulated by the
metabolic status of the cell. This review highlights studies linking KATs to metabolism. We cover
newly identified acyl-modifications (propionylation and butyrylation), discuss the control of KAT
activity by cellular acetyl-CoA levels, and provide insights into how acetylation regulates
metabolic proteins. Lastly, we conclude with a discussion of the current approaches for identifying
novel KATs and their metabolic substrates.
Keywords
Histone acetyltransferase (HAT); Lysine acetyltransferase (KAT); meta