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Putative O-glycosylation Modification Sites of Tsr Are Involved in E. coli Motility
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- Author / Creator
- Vouronikos, Bill Chris
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Post-translational modifications (PTMs) regulate a variety of normal cellular processes, many of which are conserved across eukaryotes and prokaryotes. One PTM, protein glycosylation with the reversible modification of O-GlcNAc, is well studied in eukaryotes. However, evidence for its existence in prokaryotes remains controversial. Investigating how post-translational modifications work in bacteria will help us understand how bacteria adapt to and survive in changing environments.
Bacterial swarming/swimming motility is mediated by the flagella, but it is the methyl- accepting chemotaxis proteins (MCPs) that control chemotaxis by sensing changes in environmental nutrient and/or waste concentrations. One of the major MCPs in E. coli is Tsr, which has four putative O-GlcNAc modification sites that are directly adjacent to five known methylation sites which are critical for function. Our hypothesis was that the four putative modification sites in Tsr affect bacterial motility. We have shown that two of the four putative modification sites are necessary for motility, as site-directed mutants have significantly reduced motility. We also showed that addition of glucose causes changes in global proteins glycosylation as well as motility. Our work has provided a foundation to investigate the existence of O-GlcNAc in prokaryotes. -
- Subjects / Keywords
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- Graduation date
- Fall 2022
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- Type of Item
- Thesis
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- Degree
- Master of Science
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- License
- This thesis is made available by the University of Alberta Library with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.