Proteomic analysis of iron and sulfur oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry
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| Year of publication | 2005 |
| Type | Conference abstract |
| MU Faculty or unit | |
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| Description | Acidithiobacillus ferrooxidans is a chemolithotrophic microorganism oxidizing ferrous iron and inorganic reduced sulfur substances. These bacteria are involved in formation of acid mine drainage and in biohydrometallurgic technologies. Both iron- and sulfur-oxidizing cells play a different role in oxidation of metal sulfides. Specific proteins can be expected for each type of iron or sulfur metabolism. For the above reasons, comparative analysis of protein composition of Acidithiobacillus ferrooxidans cells grown on elemental sulfur and ferrous iron was performed. Newly developed protocol involving two-dimensional gel electrophoresis with immobilized pH gradients, improved protein reduction, mass spectrometry protein identification and full genome information was applied. It 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. Many physiologically important proteins were detected using peptide mass fingerprinting and LC-MS/MS. The most interestingly, sulfate adenylytransferase involved in sulfate assimilation and sulfide dehydrogenase are between them. Many other proteins were related to important metabolic processes like substrate sorption, electron transport and inorganic ion transport. Detailed view of phosphate and sulfate transporters indicated possible interaction and/or cooperation of these proteins, as well as their post-translational modifications. |
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