Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry

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Authors

BOUCHAL Pavel ZDRÁHAL Zbyněk HELÁNOVÁ Šárka JANICZEK Oldřich HALLBERG Kevin B. MANDL Martin

Year of publication 2006
Type Article in Periodical
Magazine / Source Proteomics
MU Faculty or unit

Faculty of Science

Citation
Web
Field Biochemistry
Keywords Acidithiobacilus ferrooxidans; Iron oxidation; Protein reduction; Proteome; Sulfur oxidation
Description 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 At. 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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