Measurement and Analysis of Lysine Acetylation by KAT Complexes In Vitro and In Vivo
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The acetylation of the ε-amine of lysine residues has significant impacts on the cellular functions of proteins. Through the combination of unbiased and targeted analysis of acetylated proteins, biological insights on lysine acetylation are now routinely generated. To help in this endeavor, we describe detailed protocols for the identification of acetylated lysine residues and the preparation of multiple reagents for the characterization of these sites in order to obtain functional insights on this widespread modification.
KeywordsLysine acetylation KAT HAT TAP LC-MS/MS
We are grateful to Yannick Doyon, Karine Jacquet, Pierre Billon, and Xue Cheng for sharing their protocols. Research in the Côté and Lambert laboratories is funded by a Discovery Grants from the Natural Sciences and Engineering Research Council of Canada (NSERC) (1304616-2017 to J.-P.L.) and a Foundation Grant from the Canadian Institutes of Health Research (CIHR) (FDN-143314 to J.C.). J.-P.L. is supported by a Junior 1 salary award from the Fonds de Recherche du Québec-Santé (FRQ-S; 251747), by an Operating Grant from the Cancer Research Society (22779) and a Leader’s Opportunity Funds from the Canada Foundation for Innovation (37454). J.C. holds a Canada Research Chair (Tier 1) in Chromatin Biology and Molecular Epigenetics.