Metabolic regulation of histone acetyltransferases by endogenous Acyl-CoA cofactors

Cover of Chemistry & Biology, Volume 22, Number 8, August 20, 2015

Unraveling the metabolic regulation of lysine acetyltransferases (KATs). Montgomery et al. detail the application of a competitive chemoproteomic strategy to quantitatively characterize the interactions of acyl-CoA metabolites with cellular KAT enzymes. These studies reveal KATs are strongly inhibited by lipid-derived CoA analogs, an interaction that may have implications for the metabolic regulation of epigenetic signaling, and highlight the power of chemoproteomics to rapidly characterize metabolic-epigenetic interactions in complex biological contexts. 

Cover design by Scientific Publications, Graphics & Media, Frederick National Laboratory for Cancer Research.

Lab/Branch/Program: 
Chemical Biology Laboratory
Citation: 

See: Metabolic Regulation of Histone Acetyltransferases by Endogenous Acyl-CoA Cofactors by David C. Montgomery#, Alexander W. Sorum#, Laura Guasch, Marc C. Nicklaus and Jordan L. Meier in Chemistry & Biology201522, 1030-1039.

#Co-first author

Published Date: 
August, 2015