ERA

Download the full-sized PDF of Deletion or substitution of conserved amino acid residues at the tip of the domain IV of Tet(O) impairs tetracycline resistanceDownload the full-sized PDF

Analytics

Share

Permanent link (DOI): https://doi.org/10.7939/R3K43N

Download

Export to: EndNote  |  Zotero  |  Mendeley

Communities

This file is in the following communities:

Graduate Studies and Research, Faculty of

Collections

This file is in the following collections:

Theses and Dissertations

Deletion or substitution of conserved amino acid residues at the tip of the domain IV of Tet(O) impairs tetracycline resistance Open Access

Descriptions

Other title
Subject/Keyword
resistance
tetracycline
Tet(O)
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Mukherjee, Oindrila
Supervisor and department
Keelan, Monika (Laboratory Medicine and Pathology)
Examining committee member and department
Tyrrell, Greg (Laboratory Medicine and Pathology)
Fahlman, Richard (Department of Biochemistry)
Pukatzki, Stefan (Medical Microbiology and Immunology)
Department
Medical Sciences-Laboratory Medicine and Pathology
Specialization

Date accepted
2011-01-11T22:03:13Z
Graduation date
2011-06
Degree
Master of Science
Degree level
Master's
Abstract
Resistance to tetracycline (Tc), an inhibitor of protein synthesis, decreases its effectiveness for the treatment of bacterial infections. Tc resistance (TcR) can be mediated by the ribosomal protection protein, Tet(O), which was first reported in Campylobacter jejuni, a cause of bacterial diarrhea worldwide. Tet(O) confers TcR by mediating Tc release from 70S ribosomes, thus restoring protein synthesis. Tet(O) is widely distributed in a variety of bacterial genera, restraining the clinical use of Tc. This thesis is the first investigation into the role of the conserved set of amino acid residues, YSPVST, occupying positions 507-512 at the tip of domain IV of Tet(O). Impaired Tc release from 70S ribosomes observed with Tet(O)mutants lacking one or more of these conserved residues suggests residues at positions 509-512 play a role in Tet(O)-mediated TcR. This study provides insight into the molecular mechanism of TcR, which is essential for the development of novel therapeutics.
Language
English
DOI
doi:10.7939/R3K43N
Rights
License granted by oindrila mukherjee (oindrila@ualberta.ca) on 2011-01-11T18:34:56Z (GMT): 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 the above terms. The author reserves all other publication and other rights in association with the copyright in the thesis, and except as herein 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.
Citation for previous publication

File Details

Date Uploaded
Date Modified
2014-04-24T23:09:04.734+00:00
Audit Status
Audits have not yet been run on this file.
Characterization
File format: pdf (Portable Document Format)
Mime type: application/pdf
File size: 5842669
Last modified: 2015:10:12 14:29:05-06:00
Filename: Mukherjee_Oindrila_Spring 2011.pdf
Original checksum: dc07f7edbf53b7c8bd23a02acd1c1f74
Well formed: true
Valid: true
File title: Untitled
Page count: 207
Activity of users you follow
User Activity Date