Abstract

Lysine acetylation is a key regulatory posttranslational modification. Function of lysine acetylation is most extensively studied in the context of epigenetic regulation of gene transcription via acetylation of histones. Recent mass spectrometry (MS)-based proteomic studies have greatly expanded our knowledge of this modification. Our laboratory is using MS-based quantitative proteomics to map the scope of acetylation in diverse organisms and to investigate its dynamic regulation in response to genetic and environmental perturbations. Furthermore, we developed novel proteomic methods to accurately quantify stoichiometry of acetylation on a proteome-wide scale. Our results show that acetylation can occur through both enzymatic and non-enzymatic mechanisms and suggest an important function of sub-cellular compartmentalization in the evolution of acetylation signaling in eukaryotes. I will discuss our recently published and ongoing efforts in understanding acetylation signaling.