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Surfactant-free purification of membrane protein complexes from bacteria : application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a
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Paulin, Sarah, Jamshad, Mohammed, Dafforn, Tim, Garcia-Lara, Jorge, Foster, Simon J., Galley, Nicola F., Roper, David I., Rosado, Helena and Taylor, Peter W. (2014) Surfactant-free purification of membrane protein complexes from bacteria : application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. Nanotechnology, Volume 25 (Number 28). Article number 285101. doi:10.1088/0957-4484/25/28/285101 ISSN 0957-4484.
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Official URL: http://dx.doi.org/10.1088/0957-4484/25/28/285101
Abstract
Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of the cell division machinery from the membrane of drug-resistant staphylococcal cells. SMA-lipid nanoparticles solubilized FtsZ-PBP2-PBP2a complexes from intact cells, demonstrating the close physical proximity of these proteins within the lipid bilayer. Exposure of bacteria to (-)-epicatechin gallate, a polyphenolic agent that abolishes ?-lactam resistance in staphylococci, disrupted the association between PBP2 and PBP2a. Thus, SMA purification provides a means to remove native integral membrane protein assemblages with minimal physical disruption and shows promise as a tool for the interrogation of molecular aspects of bacterial membrane protein structure and function.
Item Type: | Journal Article | ||||||||||
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Subjects: | Q Science > QR Microbiology R Medicine > RC Internal medicine |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||
Library of Congress Subject Headings (LCSH): | Staphylococcus aureus, Drug resistance in microorganisms | ||||||||||
Journal or Publication Title: | Nanotechnology | ||||||||||
Publisher: | Institute of Physics Publishing Ltd. | ||||||||||
ISSN: | 0957-4484 | ||||||||||
Official Date: | 18 July 2014 | ||||||||||
Dates: |
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Volume: | Volume 25 | ||||||||||
Number: | Number 28 | ||||||||||
Article Number: | Article number 285101 | ||||||||||
DOI: | 10.1088/0957-4484/25/28/285101 | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||||
Date of first compliant deposit: | 28 December 2015 | ||||||||||
Date of first compliant Open Access: | 28 December 2015 | ||||||||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Royal Pharmaceutical Society of Great Britain, University College London Hospitals Foundation NHS Trustβ (UCLHFT) | ||||||||||
Grant number: | BB/1005579/1 (BBSRC) | ||||||||||
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