dc.creatorGrand, Maxime
dc.creatorBlancato, Victor Sebastian
dc.creatorEspariz, Martin
dc.creatorDeutscher, Josef
dc.creatorPikis, Andreas
dc.creatorHartke, Axel
dc.creatorMagni, Christian
dc.creatorSauvageot, Nicolas
dc.date.accessioned2022-02-03T18:50:43Z
dc.date.accessioned2022-10-15T11:20:13Z
dc.date.available2022-02-03T18:50:43Z
dc.date.available2022-10-15T11:20:13Z
dc.date.created2022-02-03T18:50:43Z
dc.date.issued2019-11
dc.identifierGrand, Maxime; Blancato, Victor Sebastian; Espariz, Martin; Deutscher, Josef; Pikis, Andreas; et al.; Enterococcus faecalis MalR acts as a repressor of the maltose operons and additionally mediates their catabolite repression via direct interaction with seryl-phosphorylated-HPr; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 113; 2; 11-2019; 464-477
dc.identifier0950-382X
dc.identifierhttp://hdl.handle.net/11336/151307
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4380119
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.languageeng
dc.publisherWiley Blackwell Publishing, Inc
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.14431
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/mmi.14431
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectMETABOLISM
dc.subjectMALTOSE
dc.subjectENTEROCOCCUS
dc.subjectREGULATION
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.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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