Enterococcus faecalis MalR acts as a repressor of the maltose operons and additionally mediates their catabolite repression via direct interaction with seryl-phosphorylated-HPr

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dc.citation.titleMolecular Microbiology
dc.citation.volume113
dc.contributor.orcidhttps://orcid.org/0000-0003-3945-2859
dc.contributor.orcidhttps://orcid.org/0000-0002-4090-515X
dc.contributor.orcidhttps://orcid.org/0000-0002-2537-0062
dc.contributor.orcidhttps://orcid.org/0000-0002-5179-9700
dc.contributor.orcidhttps://orcid.org/0000-0002-7595-4330
dc.contributor.otherBrückner, Reinhold: provide plasmid pRB473
dc.contributor.otherThompson, John: provide phosphorylated sugars
dc.creatorGrand, Maxime
dc.creatorBlancato, Víctor Sebastián
dc.creatorEspariz, Martín
dc.creatorDeutscher, Josef
dc.creatorPikis, Andreas
dc.creatorHartke, Axel
dc.creatorMagni, Christian
dc.creatorSauvageot, Nicolas
dc.date.accessioned2024-06-19T12:05:07Z
dc.date.available2024-06-19T12:05:07Z
dc.date.issued2019-11-22
dc.description.abstractEnterococci are gram-positive pathogens and lead to cause hospital-acquired infections worldwide. Central carbon metabolism was shown as highly induced in Enterococcus faecalis during infection context. Metabolism of α-polysaccharides was previously described as an important factor for host colonisation and biofilm formation. A better characterisation of the adaptation of this bacterium to carbohydrate availabilities may lead to a better understanding of the link between carbohydrate metabolism and the infection process of E. faecalis. Here we show that MalR, a LacI/GalR transcriptional regulator, is the main factor in the regulation of the two divergent operons involved in maltose metabolism in this bacterium. The malR gene is transcribed from the malP promoter, but also from an internal promoter inside the gene located upstream of malR. In the absence of maltose, MalR acts as a repressor and in the presence of glucose, it exerts efficient CcpA-independent carbon catabolite repression. The central PTS protein P-Ser-HPr interacts directly with MalR and enhances its DNA binding capacity, which allows E. faecalis to adapt its metabolism to environmental conditions.
dc.description.filFil: Grand, Maxime. Université de Caen Normandie; France.
dc.description.filFil: Blancato, Víctor Sebastián. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Espariz, Martín. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Deutscher, Josef. Université Paris-Saclay. Institut national de recherche pour l'agriculture, l'alimentation et l'environnement (INRAE). Institut Micalis; France.
dc.description.filFil: Deutscher, Josef. Université Paris-Saclay. AgroParisTech; France.
dc.description.filFil: Deutscher, Josef. Université Paris Cité. Centre national de la recherche scientifique (CNRS). Institut de biologie physico-chimique (IBPC). Laboratoire de l'Expression Génétique Microbienne (UMR 8261); France.
dc.description.filFil: Pikis, Andreas. Food and Drug Administration (FDA). Center for Drug Evaluation and Research (CDER); United States.
dc.description.filFil: Pikis, Andreas. National Institute of Health (NIH). National Institute of Dental and Craniofacial Research (NIDCR). Microbial Biochemistry and Genetics Unit; United States.
dc.description.filFil: Pikis, Andreas. National Institute of Health (NIH). National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK). Laboratory of Cellular and Developmental Biology; United States.
dc.description.filFil: Hartke, Axel. Université de Caen Normandie; France.
dc.description.filFil: Magni, Christian. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Sauvageot, Nicolas. Université de Caen Normandie; France.
dc.description.sponsorshipEuropean Union and the Normandy County Council: ERDF-ESF operational programme 2014-2020
dc.description.sponsorshipFrench Ministry of Education, Research and Innovation
dc.description.versionpeerreviewed
dc.format.extent1-14
dc.identifier.e-issn1365-2958
dc.identifier.issn0950-382X
dc.identifier.urihttps://hdl.handle.net/2133/27324
dc.language.isoen
dc.publisherWiley
dc.relation.publisherversionhttps://doi.org/10.1111/mmi.14431
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/10.1111/mmi.14431
dc.rightsopenAccess
dc.rights.holderGrand, Maxime
dc.rights.holderBlancato, Víctor Sebastián
dc.rights.holderEspariz, Martín
dc.rights.holderDeutscher, Josef
dc.rights.holderPikis, Andreas
dc.rights.holderHartke, Axel
dc.rights.holderMagni, Christian
dc.rights.holderSauvageot, Nicolas
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectEnterococcus
dc.subjectMaltose
dc.subjectMetabolism
dc.subjectRegulation
dc.subjectOperon
dc.subjectCatabolite repression
dc.subjectMalR
dc.subjectTranscriptional regulator
dc.titleEnterococcus faecalis MalR acts as a repressor of the maltose operons and additionally mediates their catabolite repression via direct interaction with seryl-phosphorylated-HPr
dc.typearticulo
dc.type.versionpublishedVersion

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