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dc.contributor.advisorGeorgiou, Georgeen
dc.contributor.committeeMemberIsaac, Sanchezen
dc.creatorChrysostomou, Constantineen
dc.date.accessioned2010-09-21T15:17:50Zen
dc.date.accessioned2010-09-21T15:17:59Zen
dc.date.accessioned2017-05-11T22:20:14Z
dc.date.available2010-09-21T15:17:50Zen
dc.date.available2010-09-21T15:17:59Zen
dc.date.available2017-05-11T22:20:14Z
dc.date.issued2009-12en
dc.date.submittedDecember 2009en
dc.identifier.urihttp://hdl.handle.net/2152/ETD-UT-2009-12-706en
dc.descriptiontexten
dc.description.abstractInhibition of disulfide bond formation in Escherichia coli implicates an intricate collaboration of proteins which comprise the glutathione and thioredoxin reducing pathways. Bioengineers have successfully engineered E. coli possessing mutated reducing pathways that promote, rather than inhibit, disulfide bond formation in the cytoplasm. The transcriptome of six such mutant E. coli strains have been characterized using Microarray technology. We find that all mutant strains, exhibit a unique response to oxidative stress, not observed in wild type. Statistical analyses revealed the expression of more than 200 genes that are affected by mutations within the reducing pathways. Significantly up-regulated biological processes include cysteine biosynthesis, histidine biosynthesis, NADH Dehydrogenase I biosynthesis, sugar catabolic processes, and activation of stress responses . The second part of this work describes the construction of an E. coli strain that promotes the complete conversion of glutathione into its seemingly dormant derivative, glutathionylspermidine. This engineered strain can be used in assays designed to evaluate the effectiveness of glutathionylspermidine as a substitute for glutathione and, hopefully, allude to its true metabolic function.en
dc.format.mimetypeapplication/pdfen
dc.language.isoengen
dc.subjectMicroarrayen
dc.subjectGlutathioneen
dc.subjectThioredoxinen
dc.subjectOxidative stressen
dc.subjectGlutathionylspermidineen
dc.titleInvestigating cellular responses to mutations in the glutathione and thioredoxin pathways of Escherichia colien
dc.type.genrethesisen
dc.date.updated2010-09-21T15:17:59Zen


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