Journal
ENVIRONMENTAL MICROBIOLOGY
Volume 19, Issue 9, Pages 3551-3566Publisher
WILEY
DOI: 10.1111/1462-2920.13848
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Funding
- Ministerio de Ciencia e Innovacion and European Region Development Fund (ERDF) [BFU2010-17946]
- Ministerio de Economia y Competitividad
- ERDF [BFU2013-43469-P, BFU2016-80122-P]
- FPI predoctoral scholarship [EEBB-BES-2011-047539]
- Engineering and Physical Sciences Research Council (United Kingdom) [EP/N006615/1]
- BBSRC [BB/R012415/1] Funding Source: UKRI
- EPSRC [EP/N006615/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/R012415/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/N006615/1] Funding Source: researchfish
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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 (5CANGGANG3) 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.
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