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Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100
Author(s) -
Watt Steven Alexander,
Wilke Andreas,
Patschkowski Thomas,
Niehaus Karsten
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200400905
Subject(s) - xanthomonas campestris , extracellular , proteome , xanthomonas campestris pv. campestris , periplasmic space , signal peptide , biochemistry , cytosol , proteomics , secretion , biology , bacterial outer membrane , trypsin , membrane protein , extracellular matrix , chemistry , peptide sequence , enzyme , membrane , escherichia coli , gene
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.