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Measurement and Analysis of Lysine Acetylation by KAT Complexes In Vitro and In Vivo

Protocol
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Part of the Methods in Molecular Biology book series (MIMB, volume 1983)

Abstract

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.

Keywords

Lysine acetylation KAT HAT TAP LC-MS/MS 

Notes

Acknowledgments

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.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.St. Patrick Research Group in Basic OncologyQuebec CityCanada
  2. 2.Laval University Cancer Research CenterQuebec CityCanada
  3. 3.Centre de Recherche du Centre Hospitalier Universitaire (CHU) de Québec-Université LavalQuebec CityCanada
  4. 4.Département de Médecine MoléculaireUniversité LavalQuebec CityCanada

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