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dc.creatorSolano Goñi, Cristinaes_ES
dc.creatorGarcía Martínez, Begoñaes_ES
dc.creatorLatasa Osta, Cristinaes_ES
dc.creatorToledo Arana, Alejandroes_ES
dc.creatorZorraquino Salvo, Violetaes_ES
dc.creatorValle Turrillas, Jaionees_ES
dc.creatorCasals, Joanes_ES
dc.creatorPedroso, Enriquees_ES
dc.creatorLasa Uzcudun, Íñigoes_ES
dc.date.accessioned2018-12-28T09:14:04Z
dc.date.available2018-12-28T09:14:04Z
dc.date.issued2009
dc.identifier.issn0027-8424 (Print)
dc.identifier.issn1091-6490 (Electronic)
dc.identifier.urihttps://hdl.handle.net/2454/31884
dc.description.abstractBacteria have developed an exclusive signal transduction system involving multiple diguanylate cyclase and phosphodiesterase domain-containing proteins (GGDEF and EAL/HD-GYP, respectively) that modulate the levels of the same diffusible molecule, 3 -5 -cyclic diguanylic acid (c-di-GMP), to transmit signals and obtain specific cellular responses. Current knowledge about c-di- GMP signaling has been inferred mainly from the analysis of recombinant bacteria that either lack or overproduce individual members of the pathway, without addressing potential compensatory effects or interferences between them. Here, we dissected c-di-GMP signaling by constructing a Salmonella strain lacking all GGDEF-domain proteins and then producing derivatives, each restoring 1 protein. Our analysis showed that most GGDEF proteins are constitutively expressed and that their expression levels are not interdependent. Complete deletion of genes encoding GGDEFdomain proteins abrogated virulence, motility, long-term survival, and cellulose and fimbriae synthesis. Separate restoration revealed that 4 proteins from Salmonella and 1 from Yersinia pestis exclusively restored cellulose synthesis in a c-di-GMP–dependent manner, indicating that c-di-GMP produced by different GGDEF proteins can activate the same target. However, the restored strain containing the STM4551-encoding gene recovered all other phenotypes by means of gene expression modulation independently of c-di-GMP. Specifically, fimbriae synthesis and virulence were recovered through regulation of csgD and the plasmid-encoded spvAB mRNA levels, respectively. This study provides evidence that the regulation of the GGDEF-domain proteins network occurs at 2 levels: a level that strictly requires c-di-GMP to control enzymatic activities directly, restricted to cellulose synthesis in our experimental conditions, and another that involves gene regulation for which c-di-GMP synthesis can be dispensable.en
dc.description.sponsorshipThis research was supported by Grants GEN2003–20234-C06–05 from Acción Estategica de Genómica y Proteómica, CTQ2007-68014-C02-01 from the Ministerio de Educación y Ciencia (Spain), and 2005SGR-693 from Generalitat de Catalunya. B.G. is the recipient of a postdoctoral contract under Grant GEN2003-20234.en
dc.format.extent6 p.
dc.format.mimetypeapplication/pdfen
dc.format.mimetypeapplication/zipen
dc.language.isoengen
dc.publisherNational Academy of Sciencesen
dc.relation.ispartofPNAS, May 12, 2009 106 (19) 7997-8002en
dc.subjectBiofilm formationen
dc.subjectSalmonella virulenceen
dc.subjectSignal transduction system celluloseen
dc.subjectSTM4551en
dc.titleGenetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonellaen
dc.typeinfo:eu-repo/semantics/articleen
dc.typeArtículo / Artikuluaes
dc.contributor.departmentIdAB - Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.identifier.doi10.1073/pnas.0812573106
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.0812573106
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dc.type.versionVersión publicada / Argitaratu den bertsioaes


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