The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR

Huertas-Rosales, Óscar, Romero, Manuel, Heeb, Stephan, Espinosa-Urgel, Manuel, Cámara, Miguel and Ramos-González, María Isabel (2017) The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR. Environmental Microbiology, 19 (9). pp. 3551-3566. ISSN 1462-2920

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Abstract

Expression of cfcR, encoding the only GGDEF/EAL response regulator in Pseudomonas putida, is transcriptionally regulated by RpoS, ANR and FleQ, and the functionality of CfcR as a diguanylate cyclase requires the multisensor CHASE3/GAF hybrid histidine kinase named CfcA. Here an additional level of cfcR control, operating post-transcriptionally via the RNA-binding proteins RsmA, RsmE and RsmI, is unraveled. Specific binding of the three proteins to an Rsm binding motif (5’CANGGANG3’) encompassing the translational start codon of cfcR was confirmed. Although RsmA exhibited the highest binding affinity to the cfcR transcript, single deletions of rsmA, rsmE or rsmI, caused minor derepression in CfcR translation compared to a ∆rsmIEA triple mutant. RsmA also showed a negative impact on c-di-GMP levels in a double mutant ∆rsmIE through the control of cfcR, which is responsible for most of the free c-di-GMP during stationary phase in static conditions. In addition, a CfcR-dependent c-di-GMP boost was observed during this stage in ∆rsmIEA confirming the negative effect of Rsm proteins on CfcR translation and explaining the increased biofilm formation in this mutant compared to the wild type. Overall these results suggest that CfcR is a key player in biofilm formation regulation by the Rsm proteins in P. putida.

Item Type: Article
RIS ID: https://nottingham-repository.worktribe.com/output/873417
Schools/Departments: University of Nottingham, UK > Faculty of Medicine and Health Sciences > School of Life Sciences
Identification Number: https://doi.org/10.1111/1462-2920.13848
Depositing User: Eprints, Support
Date Deposited: 26 Jun 2017 11:11
Last Modified: 04 May 2020 18:56
URI: https://eprints.nottingham.ac.uk/id/eprint/43763

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