title: The proteome and lipidome of Synechocystis sp. PCC 6803 cells grown under light-activated heterotrophic conditions.
abstract: Cyanobacteria are photoautotrophic prokaryotes with a plant-like photosynthetic machinery. Because of their short generation times, the ease of their genetic manipulation, and the limited size of their genome and proteome, cyanobacteria are popular model organisms for photosynthetic research. Although the principal mechanisms of photosynthesis are well-known, much less is known about the biogenesis of the thylakoid membrane, hosting the components of the photosynthetic, and respiratory electron transport chain in cyanobacteria. Here we present a detailed proteome analysis of the important model and host organism Synechocystis sp. PCC 6803 under light-activated heterotrophic growth conditions. Because of the mechanistic importance and severe changes in thylakoid membrane morphology under light-activated heterotrophic growth conditions, a focus was put on the analysis of the membrane proteome, which was supported by a targeted lipidome analysis. In total, 1528 proteins (24.5% membrane integral) were identified in our analysis. For 641 of these proteins quantitative information was obtained by spectral counting. Prominent changes were observed for proteins associated with oxidative stress response and protein folding. Because of the heterotrophic growth conditions, also proteins involved in carbon metabolism and C/N-balance were severely affected. Although intracellular thylakoid membranes were significantly reduced, only minor changes were observed in their protein composition. The increased proportion of the membrane-stabilizing sulfoqinovosyl diacyl lipids found in the lipidome analysis, as well as the increased content of lipids with more saturated acyl chains, are clear indications for a coordinated synthesis of proteins and lipids, resulting in stabilization of intracellular thylakoid membranes under stress conditions.
authors.affiliation: From the ‡Plant Biochemistry, Faculty of Biology & Biotechnology, Ruhr-University Bochum, 44780 Bochum, Germany;
authors.forename: Nicole
authors.initials: N
authors.lastname: Plohnke
authors.affiliation: §Department of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, 55128 Mainz, Germany;
authors.forename: Tobias
authors.initials: T
authors.lastname: Seidel
authors.affiliation: ¶Department of Molecular Cell Biology, Bielefeld University, 33615 Bielefeld, Germany.
authors.forename: Uwe
authors.initials: U
authors.lastname: Kahmann
authors.affiliation: From the ‡Plant Biochemistry, Faculty of Biology & Biotechnology, Ruhr-University Bochum, 44780 Bochum, Germany;
authors.forename: Matthias
authors.initials: M
authors.lastname: Rögner
authors.affiliation: §Department of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, 55128 Mainz, Germany; Sascha.Rexroth@ruhr-uni-bochum.de dirk.schneider@uni-mainz.de.
authors.forename: Dirk
authors.initials: D
authors.lastname: Schneider
authors.affiliation: From the ‡Plant Biochemistry, Faculty of Biology & Biotechnology, Ruhr-University Bochum, 44780 Bochum, Germany; Sascha.Rexroth@ruhr-uni-bochum.de dirk.schneider@uni-mainz.de.
authors.forename: Sascha
authors.initials: S
authors.lastname: Rexroth
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis*; D002244:Carbon / Q000378:metabolism; D002853:Chromatography, Liquid / Q000379:methods; D013058:Mass Spectrometry / Q000379:methods; D008563:Membrane Lipids / Q000032:analysis*; D018384:Oxidative Stress; D052817:Phototrophic Processes; D017510:Protein Folding; D020543:Proteome / Q000032:analysis*; D046939:Synechocystis / Q000254:growth & development* / Q000378:metabolism; D020524:Thylakoids / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008563:Membrane Lipids; D020543:Proteome; D002244:Carbon