Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae

• Published in: Electrophoresis Vol. 31; no. 17; pp. 2869 - 2881
• Main Authors: Ohlmeier, Steffen, Hiltunen, J. Kalervo, Bergmann, Ulrich
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 01.09.2010; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: cAMP-dependent protein kinase; Cell Respiration - physiology; cyclin-dependent kinase; Diauxic shift; electron transport chain; electrophoresis; Electrophoresis, Gel, Two-Dimensional; Fermentation; Fermentation - physiology; glucose; Metabolic Networks and Pathways - physiology; Mitochondria; Mitochondrial Proteins - chemistry; Mitochondrial Proteins - metabolism; Phosphoproteins - chemistry; Phosphoproteins - metabolism; Phosphorylation; protein phosphorylation; proteins; proteome; Proteome - chemistry; Proteome - metabolism; proteomics; pyruvate dehydrogenase (lipoamide); Respiration; Saccharomyces cerevisiae; Saccharomyces cerevisiae - metabolism; Signal Transduction - physiology; tricarboxylic acid cycle; yeasts
• ISSN: 0173-0835; 1522-2683; 1522-2683
• DOI: 10.1002/elps.200900759

Phosphorylation as a posttranslational protein modification is a common subject of proteomic studies, but phosphorylation in mitochondria is still poorly investigated. The study presented here applied 2-DE to characterize phosphorylation in the yeast mitochondrial proteome and identified 59 spots corresponding to 34 phosphorylated mitochondrial or mitochondria-associated proteins. Most of these proteins presented putative substrates of mitogen-activated protein and target of rapamycin kinases, cAMP-dependent protein kinase, cyclin-dependent kinases and Snf1p suggesting them as key players in the phosphorylation of mitochondrial or mitochondria-associated proteins. The dynamic behaviour of the phosphoproteome under a major metabolic change, the shift from fermentation to respiration (diauxic shift), was further studied. Eight proteins (Ald4p, Eft1p/2p, Eno1p, Eno2p, Om14p, Pda1p, Qcr2p, Sdh1p) had growth dependent changes in their phosphorylation, indicating a role of phosphorylation-dependent regulation of translation, metabolic pathways (e.g. glucose fermentation, tricarboxylic acid cycle, pyruvate dehydrogenase and its bypass) and respiratory chain.