Updated PubMed. Here, we performed a mass spectrometry-based analysis to study lysine acetylation and proteome dynamics in Chlamydomonas under varying growth conditions. Liquid cultures of Chlamydomonas were transferred from mixotrophic (light and acetate as carbon source) to heterotrophic (dark and acetate), or photoautotrophic (light only) growth conditions for 30 h before harvest. The proteome and acetylome changes between the different growth conditions were quantified using a stable isotope based dimethyl-labelling technique. The presence of lysine acetylation on nearly all enzymes involved in the glyoxylate cycle and its dynamic regulation in dependence on acetate was one of the major results of this study. Our results clearly show that lysine acetylation is dynamically regulated in Chlamydomonas in dependence on light and acetate. Furthermore, the newly identified lysine acetylation sites have a great potential for genetic engineering of metabolic pathways in Chlamydomonas.