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http://purl.uniprot.org/citations/18573176http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18573176http://www.w3.org/2000/01/rdf-schema#comment"

Summary

An unusual regulatory mechanism involving two response regulators, CheY1 and CheY2, but no CheZ phosphatase, operates in the chemotactic signalling chain of Sinorhizobium meliloti. Active CheY2-P, phosphorylated by the cognate histidine kinase, CheA, is responsible for flagellar motor control. In the absence of any CheZ phosphatase activity, the level of CheY2-P is quickly reset by a phospho-transfer from CheY2-P first back to CheA, and then to CheY1, which acts as a phosphate sink. In studying the mechanism of this phosphate shuttle, we have used GFP fusions to show that CheY2, but not CheY1, associates with CheA at a cell pole. Cross-linking experiments with the purified proteins revealed that both CheY2 and CheY2-P bind to an isolated P2 ligand-binding domain of CheA, but CheY1 does not. The dissociation constants of CheA-CheY2 and CheA-CheY2-P indicated that both ligands bind with similar affinity to CheA. Based on the NMR structures of CheY2 and CheY2-P, their interactions with the purified P2 domain were analysed. The interacting surface of CheY2 comprises its C-terminal beta4-alpha4-beta5-alpha5 structural elements, whereas the interacting surface of CheY2-P is shifted towards the loop connecting beta5 and alpha5. We propose that the distinct CheY2 and CheY2-P surfaces interact with two overlapping sites in the P2 domain that selectively bind either CheY2 or CheY2-P, depending on whether CheA is active or inactive."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2008.06342.x"xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Kalbitzer H.R."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Scharf B."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Schmitt R."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Haslbeck M."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Maurer T."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Riepl H."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/author"Meier V.M."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/name"Mol Microbiol"xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/pages"1373-1384"xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/title"Interaction of CheY2 and CheY2-P with the cognate CheA kinase in the chemosensory-signalling chain of Sinorhizobium meliloti."xsd:string
http://purl.uniprot.org/citations/18573176http://purl.uniprot.org/core/volume"69"xsd:string
http://purl.uniprot.org/citations/18573176http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18573176
http://purl.uniprot.org/citations/18573176http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18573176
http://purl.uniprot.org/uniprot/#_Q52880-mappedCitation-18573176http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18573176
http://purl.uniprot.org/uniprot/Q52880http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18573176