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Permanent link (DOI): https://doi.org/10.7939/R3794117W

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The Cpx pathway causes changes in peptidoglycan structure, turnover, and recycling Open Access

Descriptions

Other title
Subject/Keyword
L,D-transpeptidases
Cpx pathway
Cell wall
peptidoglycan
E. coli
stress responses
Lytic transglycosylase
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Bernal, María Margarita
Supervisor and department
Raivio, Tracy (Biological Sciences)
Examining committee member and department
Stein, Lisa (Biological Sciences)
Szymanski, Christine (Biological Sciences)
Owttrim, George (Biological Sciences)
Department
Department of Biological Sciences
Specialization
Microbiology and Biotechnology
Date accepted
2014-01-31T08:51:57Z
Graduation date
2014-06
Degree
Master of Science
Degree level
Master's
Abstract
Bacteria need to adapt to the ever-changing conditions in the environment and Escherichia coli employs the Cpx two-component system to protect the envelope, which consists of the inner membrane, periplasm, peptidoglycan, and outer membrane. Cpx is known to sense and respond to protein misfolding in the periplasm and changes to the inner membrane. In this study, we investigate the effect of the activation of the Cpx pathway on the peptidoglycan (PG) structure. We confirm the CpxR-mediated regulation of amiA, amiC, dacC, slt, mltB, ygaU, and ycbB using luminescent reporters. In addition, we confirm that these genes are activated in response to Cpx-inducing conditions. HPLC analysis shows that activation of four genes – ycbB, ygaU, slt70 and mltB - leads to changes in peptidoglycan cross-linking and turn over. Furthermore, absence of ycbB and ygaU caused activation of the Cpx pathway, suggesting that changes in PG can induce this stress response.
Language
English
DOI
doi:10.7939/R3794117W
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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