Biophysical studies of the universally conserved NTPases HflX and YchF

Simple item page
dc.contributor.authorBrandon, Harland Edward
dc.contributor.authorUniversity of Lethbridge. Faculty of Arts and Science
dc.contributor.supervisorWieden, Hans-Joachim
dc.date.accessioned2021-09-02T16:36:25Z
dc.date.available2021-09-02T16:36:25Z
dc.date.issued2021
dc.degree.levelPh.Den_US
dc.description.abstractAntibiotic resistance is becoming an increasing global health concern. The bacterial protein synthesis machinery, including the ribosome and its associated factors, are the target of over half of the clinically relevant antibiotics currently in use, highlighting the importance of cellular protein production as antibiotic target. The ribosome associated factors HflX and YchF are members of the GTPase superfamily. Their cellular functions are only poorly understood. The overarching goal of this thesis was to determine the location where HflX and YchF bind on the bacterial ribosome. Data presented here confirm that YchF interacts with the ribosomal A-site, while HflX is unique within the GTPase family being able to bind to both the ribosomal A-site and E-site. From this data and subsequent biochemical and biophysical studies, a mechanism for both HflX and YchF function during protein synthesis, specifically under stress conditions, is proposed.en_US
dc.identifier.urihttps://hdl.handle.net/10133/6013
dc.language.isoen_USen_US
dc.proquest.subject0487en_US
dc.proquest.subject0786en_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.subjectHflXen_US
dc.subjectYchFen_US
dc.subjectbacterial ribosomeen_US
dc.subjectprotein synthesisen_US
dc.subjectantibiotic resistance mechanismsen_US
dc.subjectNTPasesen_US
dc.subjectDrug resistance in microorganisms -- Researchen_US
dc.subjectBacterial proteins -- Synthesis -- Researchen_US
dc.subjectRibosomes -- Researchen_US
dc.subjectRibosomes -- Structureen_US
dc.subjectGuanosine triphosphataseen_US
dc.subjectAdenosine triphosphataseen_US
dc.subjectDissertations, Academicen_US
dc.titleBiophysical studies of the universally conserved NTPases HflX and YchFen_US
dc.typeThesisen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
BRANDON_HARLAND_PHD_2021.pdf
Size:
15.98 MB
Format:
Adobe Portable Document Format
Description:
Thesis and Appendix
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
3.25 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Arts and Science, Faculty of
University of Lethbridge Theses