Analyzing the Homodimeric and Heteromeric Nature of the Osmosensory Transporter ProP from Escherichia coli

dc.contributor.advisorWood, Janet M.
dc.contributor.authorSahtout, Naheda Mohamad Fayez
dc.date.accessioned2013-08-22T18:04:23Z
dc.date.available2013-08-22T18:04:23Z
dc.date.copyright2013-08
dc.date.created2013-08-19
dc.date.issued2013-08-22
dc.degree.departmentDepartment of Molecular and Cellular Biologyen_US
dc.degree.grantorUniversity of Guelphen_US
dc.degree.nameMaster of Scienceen_US
dc.degree.programmeMolecular and Cellular Biologyen_US
dc.description.abstractIn this study, the homodimeric and heteromeric nature of ProP, an H+/solute symporter, from E. coli was analyzed. The measured initial rates of proline uptake via ProP-His6 and His6-ProP indicated that as the growth medium osmolality increased, the assay medium osmolality required for half maximal transport activity (Π½/RT) increased and the maximal uptake rate (Amax) decreased. The oligomeric state of ProP, as determined by Blue Native PAGE, showed that both monomeric and dimeric forms of the transporter were present in wild type and cardiolipin deficient bacteria expressing ProP, ProP-His6 or His6-ProP, after culturing in low or high growth medium osmolality. The BACTH System was used to confirm the homodimeric ProP-ProP interaction and to verify the heteromeric interaction between ProP and YdhP. Initial rates of proline uptake via ProP and Western blots indicated that replacement of the ydhP locus with a kanamycin cassette had no effect on ProP function or expression.en_US
dc.identifier.urihttp://hdl.handle.net/10214/7410
dc.language.isoenen_US
dc.publisherUniversity of Guelphen_US
dc.rights.licenseAll items in the Atrium are protected by copyright with all rights reserved unless otherwise indicated.
dc.subjectEscherichia colien_US
dc.subjectProPen_US
dc.subjectOsmosensory Transporteren_US
dc.titleAnalyzing the Homodimeric and Heteromeric Nature of the Osmosensory Transporter ProP from Escherichia colien_US
dc.typeThesisen_US

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