The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus

dc.contributor.authorCaballero Sánchez, Carlos
dc.contributor.authorMenéndez Gil, Pilar
dc.contributor.authorCatalán Moreno, Arancha
dc.contributor.authorVergara Irigaray, Marta
dc.contributor.authorGarcía Martínez, Begoña
dc.contributor.authorSegura, Víctor
dc.contributor.authorIrurzun Domínguez, Naiara
dc.contributor.authorVillanueva San Martín, Maite
dc.contributor.authorRuiz de los Mozos Aliaga, Igor
dc.contributor.authorSolano Goñi, Cristina
dc.contributor.authorLasa Uzcudun, Íñigo
dc.contributor.authorToledo Arana, Alejandro
dc.contributor.departmentIdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes_ES
dc.contributor.funderUniversidad Pública de Navarra / Nafarroako Unibertsitate Publikoaes
dc.date.accessioned2018-09-06T12:20:12Z
dc.date.available2018-09-06T12:20:12Z
dc.date.issued2018
dc.description.abstractRNA-binding proteins (RBPs) are essential to finetune gene expression. RBPs containing the coldshock domain are RNA chaperones that have been extensively studied. However, the RNA targets and specific functions for many of them remain elusive. Here, combining comparative proteomics and RBPimmunoprecipitation- microarray profiling, we have determined the regulon of the RNA chaperone CspA of Staphylococcus aureus. Functional analysis revealed that proteins involved in carbohydrate and ribonucleotide metabolism, stress response and virulence gene expression were affected by cspA deletion. Stress-associated phenotypes such as increased bacterial aggregation and diminished resistance to oxidative-stress stood out. Integration of the proteome and targetome showed that CspA posttranscriptionally modulates both positively and negatively the expression of its targets, denoting additional functions to the previously proposed translation enhancement. One of these repressed targets was its own mRNA, indicating the presence of a negative post-transcriptional feedback loop. CspA bound the 5 UTR of its own mRNA disrupting a hairpin, which was previously described as an RNase III target. Thus, deletion of the cspA 5 UTR abrogated mRNA processing and auto-regulation. We propose that CspA interacts through a U-rich motif, which is located at the RNase III cleavage site, portraying CspA as a putative RNase III-antagonist.en
dc.description.sponsorshipEuropean Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme [646869]; Spanish Ministry of Economy and Competitiveness [BFU2011-23222, BIO2014-53530-R, BFU2014-56698-P]; Spanish National Research Council [CSIC-PII-201540I013]; C.J.C. was supported by predoctoral contract from the Public University of Navarre (UPNA), Spain. Funding for open access charge: European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme [646869].en
dc.format.mimetypeapplication/pdfen
dc.identifier.doi10.1093/nar/gkx1284
dc.identifier.issn0305-1048 (Print)
dc.identifier.issn1362-4962 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/30527
dc.language.isoengen
dc.publisherOxford University Pressen
dc.relation.ispartofNucleic Acids Research, 2018, Vol. 46, No. 3 1345–1361en
dc.relation.projectIDinfo:eu-repo/grantAgreement/European Commission/Horizon 2020 Framework Programme/646869/
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/6PN/BFU2011-23222/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//BIO2014-53530-R/ES/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//BFU2014-56698-P/ES/
dc.relation.publisherversionhttps://doi.org/10.1093/nar/gkx1284
dc.rights© The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.comen
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.subjectRNA chaperone CspAen
dc.subjectStaphylococcus aureusen
dc.titleThe regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureusen
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublication
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