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dc.contributor.advisorRandall, Linda L.eng
dc.contributor.authorCooper, Dylan Benjamin Joneseng
dc.date.issued2008eng
dc.date.submitted2008 Springeng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.descriptionTitle from title screen of research.pdf file (viewed on August 28, 2008)eng
dc.descriptionVita.eng
dc.descriptionThesis (M.S.) University of Missouri-Columbia 2008.eng
dc.description.abstractFor more than 3 decades, the biochemical details of the Sec system of protein export have been teased out of Escherichia coli. Through these efforts we know that SecA, the ATPase of the Sec system, interacts with several entities: unfolded precursor polypeptides, the molecular chaperone SecB, membrane phospholipids, and the membrane-embedded translocase SecYEG. Functional studies implied that some of these interactions occurred simultaneously. However, little is known about the details of these binding sites, and it was not clear to what extent SecA interacted with these diverse ligands at distinct, adjacent or overlapping surfaces along its extended structure. We investigated these issues using electron paramagnetic resonance (EPR) spectroscopy and site-directed spin labels at a multitude of sites on the surface of the 102 kDa SecA protein. EPR spectroscopy is sensitive to changes in the local environment of the spin label, and thus our survey of the SecA surface provided a map of interaction sites with its partners in the Sec pathway of protein export. Strikingly, we found that SecA utilizes a single interactive surface to bind its multiple partners during protein export. Knowing the locations and relationships of these binding sites on the surface of SecA represents significant progress in revealing the mechanistic steps of passing an unfolded polypeptide chain from SecB to SecA and ultimately driving it through the secretion pore.eng
dc.description.bibrefIncludes bibliographical references.eng
dc.identifier.merlinb64593411eng
dc.identifier.oclc244574203eng
dc.identifier.urihttps://doi.org/10.32469/10355/5660eng
dc.identifier.urihttps://hdl.handle.net/10355/5660
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcommunityUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.rightsOpenAccess.eng
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.
dc.sourceSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subjectprotein export.eng
dc.subjectprotein exporteng
dc.subject.lcshAdenosine triphosphataseeng
dc.subject.lcshElectron paramagnetic resonance spectroscopyeng
dc.subject.lcshCarrier proteinseng
dc.subject.lcshEscherichia colieng
dc.titleA study of SecA : the motor of the bacterial secretion system by site-directed spin labeling and EPReng
dc.typeThesiseng
thesis.degree.disciplineBiochemistry (Agriculture) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelMasterseng
thesis.degree.nameM.S.eng


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