Protein composition of Paracoccus denitrificans cells grown on various electron acceptors and in the presence of azide
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Sodium Azide chemistry MeSH
- Bacterial Proteins chemistry metabolism MeSH
- Databases, Protein MeSH
- Electrons * MeSH
- Mass Spectrometry MeSH
- Enzyme Inhibitors chemistry MeSH
- Membrane Proteins chemistry MeSH
- Nitrite Reductases chemistry metabolism MeSH
- Paracoccus denitrificans chemistry cytology physiology MeSH
- Proteome analysis MeSH
- Subcellular Fractions chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Sodium Azide MeSH
- Bacterial Proteins MeSH
- Enzyme Inhibitors MeSH
- Membrane Proteins MeSH
- Nitrite Reductases MeSH
- Proteome MeSH
Two-dimensional gel electrophoresis (2-DE) with immobilized pH gradients was carried out on total cell lysates and membrane fractions of Paracoccus denitrificans with the aim to characterize differences in protein expression during growth under aerobic and various anaerobic conditions (with nitrate, nitrite or nitrous oxide). Comparative image analysis of the protein pattern revealed several subgroups of the total 800 protein spots resolved that were characteristically induced or repressed in response to individual electron acceptors. The respiratory inhibitor azide also exerted a profound influence upon cellular protein composition. However, since most of the proteins showing an altered expression pattern in cells growing on oxygen differed from those in cells growing on nitrite, we suppose that azide acts mainly indirectly, possibly by influencing other cellular signals. Limited information on the P. denitrificans genome has precluded the identification of more than eight protein spots as yet. A public accessible P. denitrificans 2-DE protein database is currently built up at http://www.mpiib-berlin.mpg.de/2D-PAGE.
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