Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100.
The extracellular proteome of Xanthomonas campestris pv. campestris (Xcc) cultivated in minimal medium was isolated from the cell-free culture supernatant and separated by two-dimensional gel electrophoresis. This technique resolved 97 clearly visible protein spots, which were excised, digested with trypsin and identified on the basis of their peptide mass fingerprints generated by matrix assisted laser desorption/ionisation-time of flight-mass spectrometry. Using this approach 87 different proteins could be distinguished. The Signal P software predicted putative signal peptides for 53% of the extracellular proteins. These proteins are probably transported over the inner membrane and are localized in the periplasm, the outer membrane or secreted into the extracellular space. Among the secreted proteins are 11 degradative enzymes, which are involved in pathogenesis of Xcc. The proteins without obvious secretion signals are known to serve functions in the cytosol. How the cytosolic proteins are delivered to the extracellular space remains unclear.
Watt
Steven Alexander
SA
Department of Genetics, Faculty of Biology, University of Bielefeld, D-33501 Bielefeld, Germany.
Wilke
Andreas
A
Patschkowski
Thomas
T
Niehaus
Karsten
K
D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D045604:Extracellular Fluid / Q000737:chemistry; D010449:Peptide Mapping; D021382:Protein Sorting Signals; D020543:Proteome / Q000032:analysis*; D012984:Software; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D016959:Xanthomonas campestris / Q000737:chemistry*
D001426:Bacterial Proteins; D021382:Protein Sorting Signals; D020543:Proteome