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Understanding the Role and Mechanism of the DedA Family of Integral Membrane Proteins in Antimicrobial Resistance

Carroll, Joseph (2018) Understanding the Role and Mechanism of the DedA Family of Integral Membrane Proteins in Antimicrobial Resistance. Master of Science by Research (MScRes) thesis, University of Kent,. (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided)

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Abstract

Membrane proteins perform critical functions such as signal transduction, ion transport, and drug efflux among many other roles. DedA are a ubiquitous family of integral membrane proteins that have been shown to be important for bacterial viability. In addition, DedA proteins contribute substantially to antimicrobial resistance in clinically relevant pathogens including Klebsiella pneumoniae, where a DedA family member was recently shown to be essential for resistance to colistin. Targeting these proteins for inhibition could sensitise bacteria to other antimicrobials, making them easier to kill. However, this quest is hampered by the lack of basic understanding of the structure of DedA, their mechanism of action, and their actual physiological role in the cell. To address the dearth of structural and functional information on the DedA family, a panel of these integral membrane proteins have been cloned into two expression systems pET and pBAD. One particular E. coli DedA homologue, YqjA, was then overexpressed, solubilized, and purified. Following this, YqjA was analyzed using size exclusion chromatography. The SEC trace obtained indicated that YqjA may function as both a monomer and a dimer, although further analysis will be required to confirm this. Future work will include x-ray crystallography, cross-linking, and mass spectrometry studies.

Item Type: Thesis (Master of Science by Research (MScRes))
Thesis advisor: Mulligan, Christopher
Divisions: Faculties > Sciences > School of Biosciences
SWORD Depositor: System Moodle
Depositing User: System Moodle
Date Deposited: 05 Sep 2019 14:10 UTC
Last Modified: 06 Feb 2020 04:19 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/76217 (The current URI for this page, for reference purposes)
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