eprintid: 10100947 rev_number: 14 eprint_status: archive userid: 608 dir: disk0/10/10/09/47 datestamp: 2020-06-16 08:39:01 lastmod: 2021-10-29 22:46:27 status_changed: 2020-06-16 08:39:01 type: article metadata_visibility: show creators_name: Nicastro, GG creators_name: Kaihami, GH creators_name: Pulschen, AA creators_name: Hernandez-Montelongo, J creators_name: Boechat, AL creators_name: de Oliveira Pereira, T creators_name: Rosa, CGT creators_name: Stefanello, E creators_name: Colepicolo, P creators_name: Bordi, C creators_name: Baldini, RL title: c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein ispublished: pub divisions: UCL divisions: B02 divisions: C08 divisions: D77 note: 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/. abstract: 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. date: 2020-02-20 date_type: published publisher: Springer Science and Business Media LLC official_url: https://doi.org/10.1038/s41598-020-59536-9 oa_status: green full_text_type: pub language: eng primo: open primo_central: open_green verified: verified_manual elements_id: 1790505 doi: 10.1038/s41598-020-59536-9 lyricists_name: Arashiro Pulschen, Andre lyricists_id: APULS50 actors_name: Arashiro Pulschen, Andre actors_id: APULS50 actors_role: owner full_text_status: public publication: Scientific Reports volume: 10 article_number: 3077 citation: Nicastro, GG; Kaihami, GH; Pulschen, AA; Hernandez-Montelongo, J; Boechat, AL; de Oliveira Pereira, T; Rosa, CGT; ... Baldini, RL; + view all <#> Nicastro, GG; Kaihami, GH; Pulschen, AA; Hernandez-Montelongo, J; Boechat, AL; de Oliveira Pereira, T; Rosa, CGT; Stefanello, E; Colepicolo, P; Bordi, C; Baldini, RL; - view fewer <#> (2020) c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein. Scientific Reports , 10 , Article 3077. 10.1038/s41598-020-59536-9 <https://doi.org/10.1038/s41598-020-59536-9>. Green open access document_url: https://discovery.ucl.ac.uk/id/eprint/10100947/1/Pseudomonas_paper.pdf