Peptidoglycan maturation controls outer membrane protein assembly

Gideon Mamou, Federico Corona, Ruth Cohen-Khait, Nicholas G. Housden, Vivian Yeung, Dawei Sun, Pooja Sridhar, Manuel Pazos, Timothy J. Knowles, Colin Kleanthous () and Waldemar Vollmer ()
Additional contact information
Gideon Mamou: South Parks Road, University of Oxford
Federico Corona: Newcastle University
Ruth Cohen-Khait: South Parks Road, University of Oxford
Nicholas G. Housden: South Parks Road, University of Oxford
Vivian Yeung: South Parks Road, University of Oxford
Dawei Sun: Genentech
Pooja Sridhar: University of Birmingham
Manuel Pazos: Newcastle University
Timothy J. Knowles: University of Birmingham
Colin Kleanthous: South Parks Road, University of Oxford
Waldemar Vollmer: Newcastle University

Nature, 2022, vol. 606, issue 7916, 953-959

Abstract: Abstract Linkages between the outer membrane of Gram-negative bacteria and the peptidoglycan layer are crucial for the maintenance of cellular integrity and enable survival in challenging environments1–5. The function of the outer membrane is dependent on outer membrane proteins (OMPs), which are inserted into the membrane by the β-barrel assembly machine6,7 (BAM). Growing Escherichia coli cells segregate old OMPs towards the poles by a process known as binary partitioning, the basis of which is unknown8. Here we demonstrate that peptidoglycan underpins the spatiotemporal organization of OMPs. Mature, tetrapeptide-rich peptidoglycan binds to BAM components and suppresses OMP foldase activity. Nascent peptidoglycan, which is enriched in pentapeptides and concentrated at septa9, associates with BAM poorly and has little effect on its activity, leading to preferential insertion of OMPs at division sites. The synchronization of OMP biogenesis with cell wall growth results in the binary partitioning of OMPs as cells divide. Our study reveals that Gram-negative bacteria coordinate the assembly of two major cell envelope layers by rendering OMP biogenesis responsive to peptidoglycan maturation, a potential vulnerability that could be exploited in future antibiotic design.

Date: 2022
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/s41586-022-04834-7 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:606:y:2022:i:7916:d:10.1038_s41586-022-04834-7

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-022-04834-7

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().