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dc.contributor.authorEutsey, Rory
dc.date.accessioned2014-03-04T01:09:01Z
dc.date.available2014-03-04T01:09:01Z
dc.date.issued2006-08
dc.identifier.othereutsey_rory_200608_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/eutsey_rory_200608_ms
dc.identifier.urihttp://hdl.handle.net/10724/23360
dc.description.abstractMutY is an adenine glycosylase that has the ability to remove adenines from adenine/7,8-dihydro-8-oxoguanine (8-oxo-G) or adenine/guanine mismatches, and plays an important role in oxidative DNA damage repair. The gastric pathogen Helicobacter pylori has a homolog of the MutY enzyme. To investigate the physiological roles of MutY in H. pylori, I characterized a mutY mutant and also purified the H. pylori MutY enzyme. The mutant has an elevated spontaneous mutation frequency when incubated at 5% O2. This effect can be amplified by exposure to atmospheric oxygen levels. Most of the mutations sequenced are GC to TA transversions. Pure H. pylori MutY has the ability to remove adenines from A/8-oxo-G mismatches, but strikingly no ability to cleave A/G mismatches. The H. pylori mutY gene was able to complement an E. coli mutY mutant. H. pylori mutY mutants are only 30% as efficient as wild-type in colonizing the stomachs of mice.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectHelicobacter pylori
dc.subjectmutY
dc.subjectDNA damage
dc.subjectoxidative stress
dc.titleRole of a MutY DNA glycosylase in combatting oxidative DNA damage in Helicobacter pylori
dc.typeThesis
dc.description.degreeMS
dc.description.departmentMicrobiology
dc.description.majorMicrobiology
dc.description.advisorRobert Maier
dc.description.committeeRobert Maier
dc.description.committeeEric Stabb
dc.description.committeeLawrence Shimkets


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