Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Acidithiobacillus metabolism MeSH
- Bacterial Proteins metabolism MeSH
- Mass Spectrometry methods MeSH
- Hydrogen-Ion Concentration MeSH
- Oxidation-Reduction MeSH
- Proteomics methods MeSH
- Sulfur metabolism MeSH
- Sulfate Adenylyltransferase metabolism MeSH
- Computational Biology methods MeSH
- Iron metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Sulfur MeSH
- Sulfate Adenylyltransferase MeSH
- Iron MeSH
A comparative analysis of the protein composition of Acidithiobacillus ferrooxidans cells grown on elemental sulfur and ferrous iron was performed. A newly developed protocol involving immobilized pH gradients, improved protein reduction, mass spectrometry protein identification and full genome sequence information was applied. This approach resulted in more than 1300 protein spots displayed in broad and basic pH ranges, the best A. ferrooxidans proteome resolution to date. A comparative image analysis revealed that the proteome was significantly influenced by the growth type, and allowed for the detection of many physiologically important proteins. Among them were sulfate adenylyltransferase and sulfide dehydrogenase, which are involved in sulfate assimilation and sulfide metabolism, respectively. Many other proteins were related to important processes like cell attachment and electron transport. Co-migration of phosphate and sulfate transport proteins was also observed.
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