c-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein

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datacite.alternateIdentifier.citationSCIENTIFIC REPORTS,Vol.10,,2020
datacite.alternateIdentifier.doi10.1038/s41598-020-59536-9
datacite.creatorNicastro, Gianlucca G.
datacite.creatorKaihami, Gilberto H.
datacite.creatorPulschen, Andre A.
datacite.creatorHernandez Montelongo, Jacobo
datacite.creatorBoechat, Ana Laura
datacite.creatorPereira, Thays de Oliveira
datacite.creatorTavares Rosa, Caio Gomes
datacite.creatorStefanello, Eliezer
datacite.creatorColepicolo, Pio
datacite.creatorBordi, Christophe
datacite.creatorBaldini, Regina L.
datacite.date2020
datacite.titlec-di-GMP-related phenotypes are modulated by the interaction between a diguanylate cyclase and a polar hub protein
dc.date.accessioned2021-04-30T17:04:11Z
dc.date.available2021-04-30T17:04:11Z
dc.description.abstractc-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.
dc.identifier.urihttp://repositoriodigital.uct.cl/handle/10925/3872
dc.language.isoen
dc.publisherNATURE PUBLISHING GROUP
dc.sourceSCIENTIFIC REPORTS
oaire.resourceTypeArticle
uct.catalogadorWOS
uct.indizacionSCI
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