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dc.contributor.authorPaglioni, Sarah
dc.date.accessioned2008-02-29T17:50:20Z
dc.date.available2008-02-29T17:50:20Z
dc.date.issued2007-05
dc.identifier.urihttp://hdl.handle.net/1853/20267
dc.description.abstractChemotaxis is one of many two-component signal transduction (TCST) systems found in cells. B. subtilis shares a very similar chemotaxis system to many other bacteria and archaea and thus studies of B. subtilis can be extrapolated to the systems in other organisms. To further elucidate the current model of chemotaxis in B. subtilis we used the yeast-two-hybrid and β-galactosidase assays to determine the interactions between CheC and CheA and also between McpB and CheY. Our results reveal the interaction of CheC with the HPT domain of the histidine kinase, CheA. Interestingly, the introduction of a mutation near the phosphatase region of CheC completely disrupts the interaction with CheA. The interaction between CheA and CheC may serve as yet another level of regulation to the system. Furthermore, we explore the possibility of the receptor itself interacting with the response regulator to also aid in the adaptation of the signal.en_US
dc.language.isoen_USen_US
dc.publisherGeorgia Institute of Technologyen_US
dc.subjectChemotaxisen_US
dc.subjectCheCen_US
dc.subjectMcpBen_US
dc.titleThe role of CheC and McpB in the chemotaxis system of Bacillus subtilisen_US
dc.typeUndergraduate Thesisen_US
dc.contributor.departmentBiology
dc.description.advisorJohn Kirby - Faculty Mentor


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