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Please use this identifier to cite or link to this item: http://hdl.handle.net/11375/6148
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dc.contributor.advisorAndrews, David W.en_US
dc.contributor.authorMillman, Jonathan S.en_US
dc.date.accessioned2014-06-18T16:34:17Z-
dc.date.available2014-06-18T16:34:17Z-
dc.date.created2010-04-09en_US
dc.date.issued2002-12en_US
dc.identifier.otheropendissertations/1479en_US
dc.identifier.other2214en_US
dc.identifier.other1267849en_US
dc.identifier.urihttp://hdl.handle.net/11375/6148-
dc.description.abstract<p>The signal recognition particle pathway cotranslationally targets polytopic proteins to the inner membrane of Escherichia coli. FtsY is the receptor that is recognized by the ribosome-nascent chain-bound signal recognition particle in the bacterial targeting reaction. At the outset of this work a major unresolved issue, and current issue of some contention is the mechanism of Fts Y assembly on the E. coli inner membrane. To clarify the nature of this process, this thesis describes the region of FtsY that binds the membrane and a site-specific cleavage event that defines this region upon membrane binding. The involvement of a specific lipid, phosphatidylethanolamine and an as-yet unidentified inner membrane protein in FtsY membrane targeting are also addressed. With this understanding of the mechanisms ofFtsY membrane assembly in E. coli, additional investigations demonstrate divergent species-specific interactions with the membrane for FtsY homologues from Bacillus subtilis and Streptomyces coelicolor. Finally, the unique amino- erminal region was determined to be essential for the function of FtsY in E. coli.</p>en_US
dc.subjectBiochemistryen_US
dc.subjectBiochemistryen_US
dc.titleCHARACTERIZATION OF MEMBRANE-BINDING BY FTSY, THE PROKARYOTE SRP RECEPTORen_US
dc.typethesisen_US
dc.contributor.departmentBiochemistryen_US
dc.description.degreeDoctor of Philosophy (PhD)en_US
Appears in Collections:Open Access Dissertations and Theses

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