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Peptidoglycan biosynthesis is driven by lipid transfer along enzyme-substrate affinity gradients

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Oluwole, Abraham O., Corey, Robin A., Brown, Chelsea M., Hernández-Rocamora, Victor M., Stansfeld, Phillip J., Vollmer, Waldemar, Bolla, Jani R. and Robinson, Carol V. (2022) Peptidoglycan biosynthesis is driven by lipid transfer along enzyme-substrate affinity gradients. Nature Communications, 13 (1). 2278. doi:10.1038/s41467-022-29836-x

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Official URL: https://doi.org/10.1038/s41467-022-29836-x

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Abstract

Maintenance of bacterial cell shape and resistance to osmotic stress by the peptidoglycan (PG) renders PG biosynthetic enzymes and precursors attractive targets for combating bacterial infections. Here, by applying native mass spectrometry, we elucidate the effects of lipid substrates on the PG membrane enzymes MraY, MurG, and MurJ. We show that dimerization of MraY is coupled with binding of the carrier lipid substrate undecaprenyl phosphate (C55-P). Further, we demonstrate the use of native MS for biosynthetic reaction monitoring and find that the passage of substrates and products is controlled by the relative binding affinities of the different membrane enzymes. Overall, we provide a molecular view of how PG membrane enzymes convey lipid precursors through favourable binding events and highlight possible opportunities for intervention.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Q Science > QR Microbiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
SWORD Depositor: Library Publications Router
Library of Congress Subject Headings (LCSH): Peptidoglycans -- Synthesis, Biosynthesis, Lipids -- Metabolism, Enzymes -- Synthesis
Journal or Publication Title: Nature Communications
Publisher: Nature Publishing Group UK
ISSN: 2041-1723
Official Date: 27 April 2022
Dates:
DateEvent
27 April 2022Published
31 March 2022Accepted
Volume: 13
Number: 1
Article Number: 2278
DOI: 10.1038/s41467-022-29836-x
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
MR/V028839/1Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
University Research FellowshipRoyal Societyhttp://dx.doi.org/10.13039/501100000288
BB/R017409/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
MR/S009213/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/P01948X/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/ R002517/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/P020232/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
Studentship[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265

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