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A chemical proteomics approach to identify c-di-GMP binding proteins in Pseudomonas aeruginosa.
Düvel, Juliane Bertinetti, Daniela Möller, Stefan Schwede, Frank Morr, Michael Wissing, Josef Radamm, Lena Zimmermann, Bastian Genieser, Hans-Gottfried
Düvel, Juliane
Bertinetti, Daniela
Möller, Stefan
Schwede, Frank
Morr, Michael
Wissing, Josef
Radamm, Lena
Zimmermann, Bastian
Genieser, Hans-Gottfried
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2012-02
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Abstract
In many bacteria, high levels of the ubiquitous second messenger c-di-GMP have been demonstrated to suppress motility and to promote the establishment of surface-adherent biofilm communities. While molecular mechanisms underlying the synthesis and degradation of c-di-GMP have been comprehensively characterized, little is known about how c-di-GMP mediates its regulatory effects. In this study, we have established a chemical proteomics approach to identify c-di-GMP interacting proteins in the opportunistic pathogen Pseudomonas aeruginosa. A functionalized c-di-GMP analog, 2'-aminohexylcarbamoyl-c-di-GMP (2'-AHC-c-di-GMP), was chemically synthesized and following its immobilization used to perform affinity pull down experiments. Enriched proteins were subsequently identified by high-resolution mass spectrometry. 2'-AHC-c-di-GMP was also employed in surface plasmon resonance studies to evaluate and quantify the interaction of c-di-GMP with its potential target molecules in vitro. The biochemical tools presented here may serve the identification of novel classes of c-di-GMP effectors and thus contribute to a better characterization and understanding of the complex c-di-GMP signaling network.
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A chemical proteomics approach to identify c-di-GMP binding proteins in Pseudomonas aeruginosa. 2012, 88 (2):229-36 J. Microbiol. Methods
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en
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1872-8359
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Archived with thanks to Journal of microbiological methods