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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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WRAP-Peptidoglycan-biosynthesis-driven-lipid-enzyme-substrate-gradients-2022.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2444Kb) | Preview |
Official URL: https://doi.org/10.1038/s41467-022-29836-x
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 | |||||||||||||||||||||||||||||||||
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| Subjects: | Q Science > QP Physiology Q Science > QR Microbiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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| 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 | |||||||||||||||||||||||||||||||||
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| 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 | |||||||||||||||||||||||||||||||||
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