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http://purl.uniprot.org/citations/36987873http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36987873http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation state-dependent interactions of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) components with transcription factors play a key role in carbon catabolite repression (CCR) by glucose in bacteria. Glucose inhibits the PTS-dependent transport of fructose and is preferred over fructose in Vibrio cholerae, but the mechanism is unknown. We have recently shown that, contrary to Escherichia coli, the fructose-dependent transcriptional regulator FruR acts as an activator of the fru operon in V. cholerae and binding of the FruR-fructose 1-phosphate (F1P) complex to an operator facilitates RNA polymerase (RNAP) binding to the fru promoter. Here we show that, in the presence of glucose, dephosphorylated HPr, a general PTS component, binds to FruR. Whereas HPr does not affect DNA-binding affinity of FruR, regardless of the presence of F1P, it prevents the FruR-F1P complex from facilitating the binding of RNAP to the fru promoter. Structural and biochemical analyses of the FruR-HPr complex identify key residues responsible for the V. cholerae-specific FruR-HPr interaction not observed in E. coli. Finally, we reveal how the dephosphorylated HPr interacts with FruR in V. cholerae, whereas the phosphorylated HPr binds to CcpA, which is a global regulator of CCR in Bacillus subtilis and shows structural similarity to FruR."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkad220"xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Lee H.Y."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Lee S.H."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Seok Y.J."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Kim M.K."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/author"Yoon C.K."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/name"Nucleic Acids Res"xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/pages"5432-5448"xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/title"HPr prevents FruR-mediated facilitation of RNA polymerase binding to the fru promoter in Vibrio cholerae."xsd:string
http://purl.uniprot.org/citations/36987873http://purl.uniprot.org/core/volume"51"xsd:string
http://purl.uniprot.org/citations/36987873http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36987873
http://purl.uniprot.org/citations/36987873http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36987873
http://purl.uniprot.org/uniprot/#_Q9KM69-mappedCitation-36987873http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36987873
http://purl.uniprot.org/uniprot/#_Q9KTD6-mappedCitation-36987873http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36987873
http://purl.uniprot.org/uniprot/Q9KM69http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36987873
http://purl.uniprot.org/uniprot/Q9KTD6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36987873