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http://purl.uniprot.org/citations/20346719http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20346719http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20346719http://www.w3.org/2000/01/rdf-schema#comment"We describe a mechanism of flagellar motor control by the bacterial signaling molecule c-di-GMP, which regulates several cellular behaviors. E. coli and Salmonella have multiple c-di-GMP cyclases and phosphodiesterases, yet absence of a specific phosphodiesterase YhjH impairs motility in both bacteria. yhjH mutants have elevated c-di-GMP levels and require YcgR, a c-di-GMP-binding protein, for motility inhibition. We demonstrate that YcgR interacts with the flagellar switch-complex proteins FliG and FliM, most strongly in the presence of c-di-GMP. This interaction reduces the efficiency of torque generation and induces CCW motor bias. We present a "backstop brake" model showing how both effects can result from disrupting the organization of the FliG C-terminal domain, which interacts with the stator protein MotA to generate torque. Inhibition of motility and chemotaxis may represent a strategy to prepare for sedentary existence by disfavoring migration away from a substrate on which a biofilm is to be formed."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2010.03.001"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2010.03.001"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Blair D.F."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Blair D.F."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Paul K."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Paul K."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Harshey R.M."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Harshey R.M."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Carlquist W.C."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Carlquist W.C."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Nieto V."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/author"Nieto V."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/pages"128-139"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/pages"128-139"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/title"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/title"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/20346719http://purl.uniprot.org/core/volume"38"xsd:string