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

Abraham O. Oluwole, Robin A. Corey, Chelsea M. Brown, Victor M. Hernández-Rocamora, Phillip J. Stansfeld, Waldemar Vollmer, Jani R. Bolla () and Carol V. Robinson ()
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Abraham O. Oluwole: University of Oxford
Robin A. Corey: University of Oxford
Chelsea M. Brown: University of Warwick
Victor M. Hernández-Rocamora: Newcastle University
Phillip J. Stansfeld: University of Oxford
Waldemar Vollmer: Newcastle University
Jani R. Bolla: The Kavli Institute for Nanoscience Discovery
Carol V. Robinson: University of Oxford

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-29836-x

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