Title
GGDEF domain as spatial on-switch for a phosphodiesterase by interaction with landmark protein HubP
Author
Tim Rick, Vanessa Kreiling, Alexander Höing, Svenja Fiedler, Timo Glatter, Wieland Steinchen, Georg Hochberg, Heike Bähre, Roland Seifert, Gert Bange, Shirley K. Knauer, Peter L. Graumann & Kai M. Thorman
Year
2022
Journal
npj Biofilms and Microbiomes
Abstract
In bacteria, the monopolar localization of enzymes and protein complexes can result in a bimodal distribution of enzyme activity between the dividing cells and heterogeneity of cellular behaviors. In Shewanella putrefaciens, the multidomain hybrid diguanylate cyclase/phosphodiesterase PdeB, which degrades the secondary messenger c-di-GMP, is located at the flagellated cell pole. Here, we show that direct interaction between the inactive diguanylate cyclase (GGDEF) domain of PdeB and the FimV domain of the polar landmark protein HubP is crucial for full function of PdeB as a phosphodiesterase. Thus, the GGDEF domain serves as a spatially controlled on-switch that effectively restricts PdeBs activity to the flagellated cell pole. PdeB regulates abundance and activity of at least two crucial surface-interaction factors, the BpfA surface-adhesion protein and the MSHA type IV pilus. The heterogeneity in c-di-GMP concentrations, generated by differences in abundance and timing of polar appearance of PdeB, orchestrates the population behavior with respect to cell-surface interaction and environmental spreading.
Full Article
Instrument
FP-8300
Keywords
enzyme, GGDEF, protein