c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein
c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein
Authors
Nicastro, Gianlucca G.
Kaihami, Gilberto H.
Pulschen, Andre A.
Hernandez Montelongo, Jacobo
Boechat, Ana Laura
Pereira, Thays de Oliveira
Tavares Rosa, Caio Gomes
Stefanello, Eliezer
Colepicolo, Pio
Bordi, Christophe
Baldini, Regina L.
Kaihami, Gilberto H.
Pulschen, Andre A.
Hernandez Montelongo, Jacobo
Boechat, Ana Laura
Pereira, Thays de Oliveira
Tavares Rosa, Caio Gomes
Stefanello, Eliezer
Colepicolo, Pio
Bordi, Christophe
Baldini, Regina L.
Authors
Date
Datos de publicaciĆ³n:
SCIENTIFIC REPORTS,Vol.10,,2020
Keywords
Collections
Abstract
c-di-GMP is a major player in the switch between biofilm and motile lifestyles. Several bacteria exhibit a large number of c-di-GMP metabolizing proteins, thus a fine-tuning of this nucleotide levels may occur. It is hypothesized that some c-di-GMP metabolizing proteins would provide the global c-di-GMP levels inside the cell whereas others would maintain a localized pool, with the resulting c-di-GMP acting at the vicinity of its production. Although attractive, this hypothesis has yet to be demonstrated in Pseudomonas aeruginosa. We found that the diguanylate cyclase DgcP interacts with the cytosolic region of FimV, a polar peptidoglycan-binding protein involved in type IV pilus assembly. Moreover, DgcP is located at the cell poles in wild type cells but scattered in the cytoplasm of cells lacking FimV. Overexpression of dgcP leads to the classical phenotypes of high c-di-GMP levels (increased biofilm and impaired motilities) in the wild-type strain, but not in a Delta fimV background. Therefore, our findings suggest that DgcP activity is regulated by FimV. The polar localization of DgcP might contribute to a local c-di-GMP pool that can be sensed by other proteins at the cell pole, bringing to light a specialized function for a specific diguanylate cyclase.