%I Springer Science and Business Media LLC
%L discovery10100947
%D 2020
%O This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
%T c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein
%X c-di-GMP is a major player in the switch between bioflm and motile lifestyles. Several bacteria exhibit
a large number of c-di-GMP metabolizing proteins, thus a fne-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 bioflm
and impaired motilities) in the wild-type strain, but not in a ΔfmV background. Therefore, our fndings
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 specifc diguanylate cyclase.
%V 10
%A GG Nicastro
%A GH Kaihami
%A AA Pulschen
%A J Hernandez-Montelongo
%A AL Boechat
%A T de Oliveira Pereira
%A CGT Rosa
%A E Stefanello
%A P Colepicolo
%A C Bordi
%A RL Baldini
%J Scientific Reports