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

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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-022-29836-x

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
ORCID:
0000-0001-8647-4781
More by this author
Role:
Author
ORCID:
0000-0001-8800-7669


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
13
Issue:
1
Article number:
2278
Publication date:
2022-04-27
Acceptance date:
2022-03-31
DOI:
EISSN:
2041-1723


Language:
English
Keywords:
Pubs id:
1255385
Local pid:
pubs:1255385
Deposit date:
2022-05-03

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