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dc.contributor.authorDEVINE, KEVINen
dc.date.accessioned2014-10-20T13:24:48Z
dc.date.available2014-10-20T13:24:48Z
dc.date.issued2010en
dc.date.submitted2010en
dc.identifier.citationJende I, Varughese KI, Devine KM, Amino acid identity at one position within the alpha1 helix of both the histidine kinase and the response regulator of the WalRK and PhoPR two-component systems plays a crucial role in the specificity of phosphotransfer., Microbiology (Reading, England), 156, Pt 6, 2010, 1848-59en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/71605
dc.descriptionPUBLISHEDen
dc.description.abstractTwo-component systems usually function as cognate pairs, thereby ensuring an appropriate response to the detected signal. The ability to exclusively phosphorylate a partner protein, often in the presence of many competing homologous substrates, demonstrates a high level of specificity that must derive from the interacting surfaces of the two-component system. Here, we identify positions within the histidine kinases and response regulators of the WalRK and PhoPR two-component systems of Bacillus subtilis that make a major contribution to the specificity of phosphotransfer. Changing the identity of the amino acid at position 11 within the alpha1 helix of WalK and at position 17 within the alpha1 helix of PhoP altered discrimination and allowed phosphotransfer to occur with the non-cognate partner. Changing amino acids at additional positions of the WalK kinase increased phosphotransfer, while changes at additional positions in PhoP only had an effect in the presence of the change at position 17. The importance of amino acid identity at these two positions is supported by the fact that the amino acid combinations of Ile and Ser in WalRK, and Leu and Gly in PhoPR, are very highly conserved among orthologues, while modelling indicates that these amino acid pairs are juxtaposed in the WalRK and PhoPR complexes.en
dc.format.extent1848-59en
dc.language.isoenen
dc.relation.ispartofseriesMicrobiology (Reading, England)en
dc.relation.ispartofseries156en
dc.relation.ispartofseriesPt 6en
dc.rightsYen
dc.subjectGeneticsen
dc.titleAmino acid identity at one position within the alpha1 helix of both the histidine kinase and the response regulator of the WalRK and PhoPR two-component systems plays a crucial role in the specificity of phosphotransfer.en
dc.typeJournal Articleen
dc.contributor.sponsorScience Foundation Ireland (SFI)en
dc.contributor.sponsorScience Foundation Ireland (SFI)en
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/kdevineen
dc.identifier.rssinternalid86621en
dc.identifier.doihttp://dx.doi.org/10.1099/mic.0.037515-0en
dc.rights.ecaccessrightsopenAccess
dc.contributor.sponsorGrantNumber08/IN.1/B1859en
dc.contributor.sponsorGrantNumber03/IN3/B409en


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