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

• Published in: Proteomics (Weinheim) 2006-08, Vol.6 (15), p.4278-4285
• Main Authors: Bouchal, Pavel, Zdráhal, Zbyněk, Helánová, Šárka, Janiczek, Oldřich, Hallberg, Kevin B., Mandl, Martin
• Format: Article
• Language: English
• Subjects: Acidithiobacillus - metabolism; Acidithiobacillus ferrooxidans; Analytical, structural and metabolic biochemistry; Bacterial Proteins - metabolism; Biological and medical sciences; Computational Biology - methods; Electrophoresis, Gel, Two-Dimensional; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Iron - metabolism; Iron oxidation; Mass Spectrometry - methods; Miscellaneous; Oxidation-Reduction; Protein reduction; Proteins; Proteome; Proteomics - methods; Sulfate Adenylyltransferase - metabolism; Sulfur - metabolism; Sulfur oxidation
• ISSN: 1615-9853; 1615-9861
• DOI: 10.1002/pmic.200500719

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.