Zitieren Sie bitte immer diesen URN: urn:nbn:de:kobv:b43-511214
Local c-di-GMP signaling in the control of synthesis of the E. coli biofilm exopolysaccharide pEtN-cellulose
- In many bacteria, the biofilm-promoting second messenger c-di-GMP is produced and degraded by multiple diguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively. High target specificity of some of these enzymes has led to theoretical concepts of "local" c-di-GMP signaling. In Escherichia coli K-12, which has 12 DGCs and 13 PDEs, a single DGC, DgcC, is specifically required for the biosynthesis of the biofilm exopolysaccharide pEtN-cellulose without affecting the cellular c-di-GMP pool, but the mechanistic basis of this target specificity has remained obscure. DGC activity of membrane-associated DgcC, which is demonstrated in vitro in nanodiscs, is shown to be necessary and sufficient to specifically activate cellulose biosynthesis in vivo. DgcC and a particular PDE, PdeK (encoded right next to the cellulose operon), directly interact with cellulose synthase subunit BcsB and with each other, thus establishing physical proximity between cellulose synthase and a local sourceIn many bacteria, the biofilm-promoting second messenger c-di-GMP is produced and degraded by multiple diguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively. High target specificity of some of these enzymes has led to theoretical concepts of "local" c-di-GMP signaling. In Escherichia coli K-12, which has 12 DGCs and 13 PDEs, a single DGC, DgcC, is specifically required for the biosynthesis of the biofilm exopolysaccharide pEtN-cellulose without affecting the cellular c-di-GMP pool, but the mechanistic basis of this target specificity has remained obscure. DGC activity of membrane-associated DgcC, which is demonstrated in vitro in nanodiscs, is shown to be necessary and sufficient to specifically activate cellulose biosynthesis in vivo. DgcC and a particular PDE, PdeK (encoded right next to the cellulose operon), directly interact with cellulose synthase subunit BcsB and with each other, thus establishing physical proximity between cellulose synthase and a local source and sink of c-di-GMP. This arrangement provides a localized, yet open source of c-di-GMP right next to cellulose synthase subunit BcsA, which needs allosteric activation by c-di-GMP. Through mathematical modeling and simulation, we demonstrate that BcsA binding from the low cytosolic c-di-GMP pool in E. coli is negligible, whereas a single c-di-GMP molecule that is produced and released in direct proximity to cellulose synthase increases the probability of c-di-GMP binding to BcsA several hundred-fold. This local c-di-GMP signaling could provide a blueprint for target-specific second messenger signaling also in other bacteria where multiple second messenger producing and degrading enzymes exist.…
Autor*innen: | Anja RichterORCiD, A. Possling, N. Malysheva, K. P. Yousef, S. Herbst, M. von Kleist, R. Hengge |
---|---|
Dokumenttyp: | Zeitschriftenartikel |
Veröffentlichungsform: | Verlagsliteratur |
Sprache: | Englisch |
Titel des übergeordneten Werkes (Englisch): | Journal of Molecular Biology |
Jahr der Erstveröffentlichung: | 2020 |
Organisationseinheit der BAM: | 4 Material und Umwelt |
4 Material und Umwelt / 4.1 Biologische Materialschädigung und Referenzorganismen | |
Veröffentlichende Institution: | Bundesanstalt für Materialforschung und -prüfung (BAM) |
Verlag: | Elsevir Ltd. |
Jahrgang/Band: | 432 |
Ausgabe/Heft: | 16 |
Erste Seite: | 4576 |
Letzte Seite: | 4595 |
DDC-Klassifikation: | Technik, Medizin, angewandte Wissenschaften / Ingenieurwissenschaften / Ingenieurwissenschaften und zugeordnete Tätigkeiten |
Freie Schlagwörter: | Bacterial second messenger; Biofilm; C-di-GMP; Cellulose synthase |
Themenfelder/Aktivitätsfelder der BAM: | Material |
DOI: | 10.1016/j.jmb.2020.06.006 |
URN: | urn:nbn:de:kobv:b43-511214 |
ISSN: | 0022-2836 |
Verfügbarkeit des Dokuments: | Datei für die Öffentlichkeit verfügbar ("Open Access") |
Lizenz (Deutsch): | Creative Commons - CC BY-NC-ND - Namensnennung - Nicht kommerziell - Keine Bearbeitungen 4.0 International |
Datum der Freischaltung: | 17.08.2020 |
Referierte Publikation: | Ja |
Datum der Eintragung als referierte Publikation: | 17.08.2020 |
Schriftenreihen ohne Nummerierung: | Wissenschaftliche Artikel der BAM |