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Phosphoproteomic Analysis of Rhodopseudomonas palustris Reveals the Role of Pyruvate Phosphate Dikinase Phosphorylation in Lipid Production
- Source :
- Journal of Proteome Research. 11:5362-5375
- Publication Year :
- 2012
- Publisher :
- American Chemical Society (ACS), 2012.
-
Abstract
- Rhodopseudomonas palustris (R. palustris) is a purple nonsulfur anoxygenic phototrophic bacterium with metabolic versatility and is able to grow under photoheterotrophic and chemoheterotrophic states. It has uses in carbon management, carbon recycling, hydrogen generation, and lipid production; therefore, it has the potential for bioenergy production and biodegradation. This study is the first to identify the phosphoproteome of R. palustris including 100 phosphopeptides from 54 phosphoproteins and 74 phosphopeptides from 42 phosphoproteins in chemoheterotrophic and photoheterotrophic growth conditions, respectively. In the identified phosphoproteome, phosphorylation at the threonine residue, Thr487, of pyruvate phosphate dikinase (PPDK, RPA1051) was found to participate in the regulation of carbon metabolism. Here, we show that PPDK enzyme activity is higher in photoheterotrophic growth, with Thr487 phosphorylation as a possible mediator. Under the same photoheterotrophic conditions, R. palustris with overexpressed wild-type PPDK showed an enhanced accumulation of total lipids than those with mutant PPDK (T487V) form. This study reveals the role of the PPDK in the production of biodiesel material, lipid content, with threonyl-phosphorylation as one of the possible regulatory events during photoheterotrophic growth in R. palustris.
- Subjects :
- Proteome
Molecular Sequence Data
Mutant
Biology
Biochemistry
Pyruvate, phosphate dikinase
Bacterial Proteins
Tandem Mass Spectrometry
Escherichia coli
Amino Acid Sequence
Cloning, Molecular
Phosphorylation
Threonine
DNA Primers
Base Sequence
General Chemistry
Phosphoproteins
biology.organism_classification
Lipids
Anoxygenic photosynthesis
Enzyme assay
Pyruvate, Orthophosphate Dikinase
Rhodopseudomonas
Mutagenesis, Site-Directed
biology.protein
Rhodopseudomonas palustris
Chromatography, Liquid
Subjects
Details
- ISSN :
- 15353907 and 15353893
- Volume :
- 11
- Database :
- OpenAIRE
- Journal :
- Journal of Proteome Research
- Accession number :
- edsair.doi.dedup.....9030d7b60a4e6bc829352c47c37e795b