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dc.contributor.authorSchwaner, William Ryan
dc.date.accessioned2014-03-03T20:22:00Z
dc.date.available2014-03-03T20:22:00Z
dc.date.issued2002-12
dc.identifier.otherschwaner_william_r_200212_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/schwaner_william_r_200212_ms
dc.identifier.urihttp://hdl.handle.net/10724/20661
dc.description.abstractChaperones play a fundamental role in facilitating the proper folding of intracellular proteins. They rescue misfolded or damaged proteins and allow them the opportunity to refold into an enzymatically active form. While previous studies of chaperone proteins have focused on in vitro folding characteristics, this research provides an intracellular examination of chaperone function by analyzing the ability of either GroELS or DnaKJ to rescue misfolded proteins in vivo. Libraries of non-functional missense mutants were obtained for the hisC and hisD genes from Salmonella typhimurium and the lacY, lacZ, and trpA genes from Escherichia coli. Overexpression vectors containing either the dnaKJ or groELS genes from E. coli were introduced into each missense mutant. Twenty-five percent of the 185 inactive missense mutants tested could be suppressed by the overproduction of either DnaKJ or GroELS. The percentage of overlap between the specific mutant alleles that could be suppressed by both chaperones was significant.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectChaperone
dc.subjectMissense
dc.subjectMutant
dc.subjectGroELS
dc.subjectDnaKJ
dc.subjectIn vivo
dc.titleCharacterization of in vivo chaperone function by the rescue of nonfunctional missense mutants
dc.typeThesis
dc.description.degreeMS
dc.description.departmentMicrobiology
dc.description.majorMicrobiology
dc.description.advisorTimothy Hoover
dc.description.committeeTimothy Hoover
dc.description.committeeEllen Neidle
dc.description.committeeWilliam Whitman


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