Insight into the universally conserved NTPases HflX and YchF

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dc.contributor.authorCoatham, Mackenzie Leigh
dc.contributor.supervisorWieden, Hans-Joachim
dc.date.accessioned2014-10-14T20:54:40Z
dc.date.available2014-10-14T20:54:40Z
dc.date.issued2014
dc.degree.levelMastersen_US
dc.degree.levelMasters
dc.description.abstractThe functional roles of the two universally conserved bacterial GTPases, HflX and YchF, are poorly understood. Both proteins associate with 70S ribosomes as well as 30S and 50S ribosomal subunits. Understanding exactly how HflX and YchF interact with the ribosome and nucleotides will be important for the discovery of the in vivo relevant ribosomal complex. Presented in this thesis, is the development of a fluorescence-based system that can be used to monitor the association of HflX to 70S, 50S and 30S. Additionally, as HflX lacks the canonical glutamine that is required for the hydrolysis of GTP and ATP, an examination into how HflX hydrolyzes purine nucleotides was conducted. Furthermore, nucleotide association and dissociation rate constants were determined in the presence of ribosomes for YchF and in the presence and absence of antibiotics for HflX. The results presented here provide additional insight into the enzymatic properties of HflX and YchF.en_US
dc.identifier.urihttps://hdl.handle.net/10133/3539
dc.language.isoenen_US
dc.proquest.subject0487en_US
dc.proquest.subject0786en_US
dc.proquest.subject0307en_US
dc.proquestyesYesen_US
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistryen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.relation.ispartofseriesThesis (University of Lethbridge. Faculty of Arts and Science)en_US
dc.subjectbacteriaen_US
dc.subjectenzymatic propertiesen_US
dc.subjectGTPasesen_US
dc.subjectHflXen_US
dc.subjectYchFen_US
dc.titleInsight into the universally conserved NTPases HflX and YchFen_US
dc.typeThesisen_US
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