RT Journal Article
SR Electronic
T1 c-di-GMP-linked phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 154005
DO 10.1101/154005
A1 Gianlucca G. Nicastro
A1 Gilberto H. Kaihami
A1 André A. Pulschen
A1 Jacobo Hernandez-Montelongo
A1 Ana Laura Boechat
A1 Thays de O. Pereira
A1 Eliezer Stefanello
A1 Pio Colepicolo
A1 Christophe Bordi
A1 Regina L. Baldini
YR 2017
UL http://biorxiv.org/content/early/2017/06/22/154005.abstract
AB c-di-GMP is a major player in the decision between biofilm and sessile lifestyles. Several bacteria present 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 was yet to be proven in Pseudomonas aeruginosa. We found that the diguanylate cyclase DgcP interacts with the cytosolic region of FimV, a 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 ΔfimV background. Therefore, our findings strongly suggest that DgcP is regulated by FimV and may provide the 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.Importance Bacteria can switch between sessile and motile lifestyles and c-di-GMP is a crucial second messenger for this decision. They present several proteins that can synthetize, degrade and sense this molecule and it is intriguing why so many apparently redundant proteins are needed. An idea is that some of these proteins may act at specific subcellular locations, leading to the formation of localized c-di-GMP pools that may control the assembly and function of polar-localized machineries such as pili and flagella. We found that DgcP, a c-di-GMP synthesizing enzyme, interacts with the type IV pili hub located at the cell poles, and this interaction modulates c-di-GMP-related phenotypes. Our findings support the hypothesis that c-di-GMP acts on targets near the spot where it is produced.