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Füßl, M.* ; König, A.-C. ; Eirich, J.* ; Hartl, M.* ; Kleinknecht, L.* ; Bohne, A.V.* ; Harzen, A.* ; Kramer, K.* ; Leister, D.* ; Nickelsen, J.* ; Finkemeier, I.*

Dynamic light- and acetate-dependent regulation of the proteome and lysine acetylome of Chlamydomonas.

Plant J. 109, 261-277 (2022)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
The green alga Chlamydomonas reinhardtii is one of the most studied microorganisms in photosynthesis research and for biofuel production. A detailed understanding of the dynamic regulation of its carbon metabolism is therefore crucial for metabolic engineering. Post-translational modifications can act as molecular switches for the control of protein function. Acetylation of the ɛ-amino group of lysine residues is a dynamic modification on proteins across organisms from all kingdoms. Here, we performed a mass spectrometry-based profiling of proteome and lysine acetylome dynamics in Chlamydomonas under varying growth conditions. Chlamydomonas liquid cultures 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. In total, 5863 protein groups and 1376 lysine acetylation sites were identified with a FDR < 1 %. As a major result of this study, our data shows that dynamic changes in abundance of lysine acetylation on various enzymes involved in photosynthesis, fatty acid metabolism, and the glyoxylate cycle are depending on acetate and light. Exemplary determination of acetylation site stoichiometries revealed particularly high occupancy levels on K175 of the large subunit of RuBisCO and K99 and K340 of peroxisomal citrate synthase, respectively, under heterotrophic conditions. The lysine acetylation stoichiometries correlated with increased activities of cellular citrate synthase, and the known inactivation of the Calvin-Benson cycle under heterotrophic conditions. In conclusion, the newly identified dynamic lysine acetylation sites may have a great potential for genetic engineering of metabolic pathways in Chlamydomonas.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Acetate ; Chlamydomonas ; Citrate Synthase ; Fatty Acid Metabolism ; Glyoxylate Cycle ; Light ; Lysine Acetylation ; Proteome ; Quantitative Ms-based Proteomics ; Rubisco; Carbon Metabolism; Oxidative Stress; Photosystem-ii; Coa Synthetase; Alpha-tubulin; Acetylation; Reinhardtii; Identification; Proteins; Quantification
ISSN (print) / ISBN 0960-7412
e-ISSN 1365-313X
Zeitschrift Plant Journal, The
Quellenangaben Band: 109, Heft: 1, Seiten: 261-277 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort 111 River St, Hoboken 07030-5774, Nj Usa
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) CF Metabolomics & Proteomics (CF-MPC)
Förderungen University of Muenster
Max-Planck Society