The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR
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 c...
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| Format: | Article |
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Wiley
2017
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| Online Access: | https://eprints.nottingham.ac.uk/43763/ |
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| author | Huertas-Rosales, Óscar Romero, Manuel Heeb, Stephan Espinosa-Urgel, Manuel Cámara, Miguel Ramos-González, María Isabel |
| author_facet | Huertas-Rosales, Óscar Romero, Manuel Heeb, Stephan Espinosa-Urgel, Manuel Cámara, Miguel Ramos-González, María Isabel |
| author_sort | Huertas-Rosales, Óscar |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T19:53:09Z |
| format | Article |
| id | nottingham-43763 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:53:09Z |
| publishDate | 2017 |
| publisher | Wiley |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-437632020-05-04T18:56:12Z https://eprints.nottingham.ac.uk/43763/ 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 Ramos-González, María Isabel 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. Wiley 2017-07-21 Article PeerReviewed 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 http://onlinelibrary.wiley.com/doi/10.1111/1462-2920.13848/full doi:10.1111/1462-2920.13848 doi:10.1111/1462-2920.13848 |
| spellingShingle | Huertas-Rosales, Óscar Romero, Manuel Heeb, Stephan Espinosa-Urgel, Manuel Cámara, Miguel Ramos-González, María Isabel The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title | The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title_full | The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title_fullStr | The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title_full_unstemmed | The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title_short | The Pseudomonas putida CsrA/RsmA homologues negatively affect c-di-GMP pools and biofilm formation through the GGDEF/EAL response regulator CfcR |
| title_sort | pseudomonas putida csra/rsma homologues negatively affect c-di-gmp pools and biofilm formation through the ggdef/eal response regulator cfcr |
| url | https://eprints.nottingham.ac.uk/43763/ https://eprints.nottingham.ac.uk/43763/ https://eprints.nottingham.ac.uk/43763/ |