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http://hdl.handle.net/11375/6148
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DC Field | Value | Language |
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dc.contributor.advisor | Andrews, David W. | en_US |
dc.contributor.author | Millman, Jonathan S. | en_US |
dc.date.accessioned | 2014-06-18T16:34:17Z | - |
dc.date.available | 2014-06-18T16:34:17Z | - |
dc.date.created | 2010-04-09 | en_US |
dc.date.issued | 2002-12 | en_US |
dc.identifier.other | opendissertations/1479 | en_US |
dc.identifier.other | 2214 | en_US |
dc.identifier.other | 1267849 | en_US |
dc.identifier.uri | http://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.subject | Biochemistry | en_US |
dc.subject | Biochemistry | en_US |
dc.title | CHARACTERIZATION OF MEMBRANE-BINDING BY FTSY, THE PROKARYOTE SRP RECEPTOR | en_US |
dc.type | thesis | en_US |
dc.contributor.department | Biochemistry | en_US |
dc.description.degree | Doctor of Philosophy (PhD) | en_US |
Appears in Collections: | Open Access Dissertations and Theses |
Files in This Item:
File | Size | Format | |
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fulltext.pdf | 6.37 MB | Adobe PDF | View/Open |
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