Professor Chuna Ram Choudhary, The Novo Nordisk Foundation Center for Protein Research, Faculty of Heath Sciences, University of Copenhagen, Denmark:

Mass spectrometry-based global analysis of the dynamics and stoichiometry of lysine acetylation

Friday 21. October, 9.15 N.B., N-terminalen

Abstract
Lysine acetylation has emerged as a frequently occurring posttranslational modification in prokaryotes and eukaryotes. Proteomic studies in human and mouse cells and tissues have identified thousands of acetylation sites in diverse proteins, prominently including many mitochondrial metabolic enzymes. In agreement with the occurrence of acetylation on diverse proteins, the enzymes involved in acetylation (i.e. acetyltransferases and deacetylases) are involved in regulating various cellular processes. Thus, information about the dynamics of acetylation and their regulatory enzymes is useful in understanding the functional relevance of this modification. In our effort to better understand the mechanisms and regulation of acetylation, we applied quantitative mass spectrometry to investigate the dynamic changes in acetylation in response to metabolic, chemical and genetic perturbations. Our results suggest a close link between metabolism and acetylation, and indicate an important role of sub-cellular organization in the evolution of acetylation signaling in eukaryotes. I will also present our recent and ongoing work for estimating the stoichiometry of acetylation, and the importance of SIRT3 in regulating acetylation of mitochondrial proteins.