Aufsatz in einer Fachzeitschrift
Application of synthetic peptide arrays to uncover c-di-GMP binding motifs
Details zur Publikation
Autor(inn)en: | Düvel, J.; Bense, S.; Möller, S.; Möller, S.; Bertinetti, D.; Schwede, F.; Morr, M.; Eckweiler, D.; Genieser, H.; Jänsch, L.; Herberg, F.; Frank, R.; Häussler, S. |
Publikationsjahr: | 2015 |
Zeitschrift: | Journal of Bacteriology |
Seitenbereich: | 138-146 |
Jahrgang/Band : | 198 |
Heftnummer: | 1 |
ISSN: | 0021-9193 |
DOI-Link der Erstveröffentlichung: |
Zusammenfassung, Abstract
In many bacterial pathogens the universal bacterial second messenger c-di-GMP governs the switch from the planktonic, motile mode of growth to the sessile, biofilm mode of growth. Bacteria adapt their intracellular c-di-GMP levels to a variety of environmental challenges. Several classes of c-di-GMP binding proteins have been structurally characterized, and diverse c-di-GMP binding domains have been identified. Nevertheless, for several c-di-GMP receptors, the binding motif remains to be determined. Here we show that the use of a synthetic peptide array allowed the identification of a c-di-GMP binding motif of a putative c-di-GMP receptor protein in the opportunistic pathogen P. aeruginosa. The application of synthetic peptide arrays will facilitate the search for additional c-di-GMP receptor proteins and aid in the characterization of c-di-GMP binding motifs.
In many bacterial pathogens the universal bacterial second messenger c-di-GMP governs the switch from the planktonic, motile mode of growth to the sessile, biofilm mode of growth. Bacteria adapt their intracellular c-di-GMP levels to a variety of environmental challenges. Several classes of c-di-GMP binding proteins have been structurally characterized, and diverse c-di-GMP binding domains have been identified. Nevertheless, for several c-di-GMP receptors, the binding motif remains to be determined. Here we show that the use of a synthetic peptide array allowed the identification of a c-di-GMP binding motif of a putative c-di-GMP receptor protein in the opportunistic pathogen P. aeruginosa. The application of synthetic peptide arrays will facilitate the search for additional c-di-GMP receptor proteins and aid in the characterization of c-di-GMP binding motifs.
