Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach
Musa YR, Baesell K, Schatschneider S, Vorhölter F-J, Becher D, Niehaus K (2013)
Journal of Biotechnology 167(2): 111-122.
Zeitschriftenaufsatz
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Autor*in
Musa, Yaarub Raji;
Baesell, Katrin;
Schatschneider, SarahUniBi;
Vorhölter, Frank-JörgUniBi;
Becher, Doerte;
Niehaus, KarstenUniBi
Einrichtung
Abstract / Bemerkung
Xanthomonas campestris pv. campestris (Xcc) synthesizes huge amounts of the exopolysaccharide xanthan and is a plant pathogen affecting Brassicaceae, among them the model plant Arabidopsis thaliana. Xanthan is produced as a thickening agent at industrial scale by fermentation of Xcc. In an approach based on 2D gel electrophoresis, protein samples from different growth phases were characterized to initialize analysis of the Xanthomonas phosphoproteome. The 2D gels were stained with Pro-Q Diamond phosphoprotein stain to identify putatively phosphorylated proteins. Spots of putatively phosphorylated proteins were excised from the gel and analyzed by mass spectrometry. Three proteins were confirmed to be phosphorylated, the phosphoglucomutase/phosphomannomutase XanA that is important for xanthan and lipopolysaccharide biosynthesis, the phosphoenolpyruvate synthase PspA that is involved in gluconeogenesis, and an anti-sigma factor antagonist RsbR that was so far uncharacterized in xanthomonads. The growth phase in which the samples were collected had an influence on protein phosphorylation in Xcc, particular distinct in case of RsbR, which was phosphorylated during the transition from the late exponential growth phase to the stationary phase. (C) 2013 Elsevier B.V. All rights reserved.
Stichworte
factor;
Anti-anti-sigma;
LPS;
EPS;
Bacteria;
Posttranslational modification
Erscheinungsjahr
2013
Zeitschriftentitel
Journal of Biotechnology
Band
167
Ausgabe
2
Seite(n)
111-122
ISSN
0168-1656
Page URI
https://pub.uni-bielefeld.de/record/2625790
Zitieren
Musa YR, Baesell K, Schatschneider S, Vorhölter F-J, Becher D, Niehaus K. Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach. Journal of Biotechnology. 2013;167(2):111-122.
Musa, Y. R., Baesell, K., Schatschneider, S., Vorhölter, F. - J., Becher, D., & Niehaus, K. (2013). Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach. Journal of Biotechnology, 167(2), 111-122. doi:10.1016/j.jbiotec.2013.06.009
Musa, Yaarub Raji, Baesell, Katrin, Schatschneider, Sarah, Vorhölter, Frank-Jörg, Becher, Doerte, and Niehaus, Karsten. 2013. “Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach”. Journal of Biotechnology 167 (2): 111-122.
Musa, Y. R., Baesell, K., Schatschneider, S., Vorhölter, F. - J., Becher, D., and Niehaus, K. (2013). Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach. Journal of Biotechnology 167, 111-122.
Musa, Y.R., et al., 2013. Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach. Journal of Biotechnology, 167(2), p 111-122.
Y.R. Musa, et al., “Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach”, Journal of Biotechnology, vol. 167, 2013, pp. 111-122.
Musa, Y.R., Baesell, K., Schatschneider, S., Vorhölter, F.-J., Becher, D., Niehaus, K.: Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach. Journal of Biotechnology. 167, 111-122 (2013).
Musa, Yaarub Raji, Baesell, Katrin, Schatschneider, Sarah, Vorhölter, Frank-Jörg, Becher, Doerte, and Niehaus, Karsten. “Dynamic protein phosphorylation during the growth of Xanthomonas campestris pv. campestris B100 revealed by a gel-based proteomics approach”. Journal of Biotechnology 167.2 (2013): 111-122.
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