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http://purl.uniprot.org/citations/12970183http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12970183http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12970183http://www.w3.org/2000/01/rdf-schema#comment"Protein-tyrosine kinases regulating bacterial exopolysaccharide synthesis autophosphorylate on tyrosines located in a conserved C-terminal region. So far no other substrates have been identified for these kinases. Here we demonstrate that Bacillus subtilis YwqD not only autophosphorylates at Tyr-228, but that it also phosphorylates the two UDP-glucose dehydrogenases (UDP-glucose DHs) YwqF and TuaD at a tyrosine residue. However, phosphorylation of YwqF and TuaD occurs only in the presence of the transmembrane protein YwqC. The presumed intracellular C-terminal part of YwqC (last 50 amino acids) seems to interact with the tyrosine-kinase and to allow YwqD-catalysed phosphorylation of the two UDP-glucose DHs, which are key enzymes for the synthesis of acidic polysaccharides. However, only when phosphorylated by YwqD do the two enzymes exhibit detectable UDP-glucose DH activity. Dephosphorylation of P-Tyr-YwqF and P-Tyr-TuaD by the P-Tyr-protein phosphatase YwqE switched off their UDP-glucose DH activity. YwqE, which is encoded by the fourth gene of the B.subtilis ywqCDEF operon, also dephosphorylates P-Tyr-YwqD."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg458"xsd:string
http://purl.uniprot.org/citations/12970183http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg458"xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Boel G."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Boel G."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Decottignies P."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Decottignies P."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Deutscher J."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Deutscher J."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Maze A."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Maze A."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Grangeasse C."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Grangeasse C."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Mijakovic I."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Mijakovic I."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Jamet E."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Jamet E."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Le Marechal P."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Le Marechal P."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Poncet S."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Poncet S."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Gillet S."xsd:string
http://purl.uniprot.org/citations/12970183http://purl.uniprot.org/core/author"Gillet S."xsd:string