Journal article
Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli
Nature microbiology, Vol.10, pp.1521-1534
05/27/2025
DOI: 10.1038/s41564-025-02011-w
PMCID: PMC13032133
PMID: 40425829
Abstract
In Escherichia coli, FtsN is thought to coordinate septal peptidoglycan (sPG) synthesis and degradation. Its E domain interacts with the sPG synthesis complex, FtsWIQLB, and its SPOR domain interacts with denuded glycan (dnG), intermediates of sPG degradation. Here we used single-molecule tracking of FtsN and FtsW to investigate how FtsN coordinates the two opposing processes. We found that the SPOR domain binds to dnG cooperatively. This binding sequesters FtsWIQLB on dnG, which we call the dnG-track, and prevents dnG degradation. SPOR domain's release from dnGs exposes dnGs to degradation, moves FtsN to the sPG synthesis track and activates FtsWIQLB. In addition, FtsN self-interacts through the SPOR domain, promoting the multimerization of FtsWIQLB on both tracks. This self-interaction may create a sensitive switch, regulating FtsN's partitioning between dnG- and sPG-tracks to coordinate sPG degradation and synthesis while also controlling the balance between sequestered and active populations of the sPG synthesis complex. Our data reveal a third track that plays an important role in sPG synthesis and degradation across space and time, complementing the previously discovered sPG-track and FtsZ-track in E. coli for robust septal cell wall constriction.
Details
- Title: Subtitle
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli
- Creators
- Zhixin Lyu - Johns Hopkins UniversityXinxing Yang - Johns Hopkins UniversityAtsushi Yahashiri - University of IowaStephen Ha - Johns Hopkins UniversityJoshua W McCausland - Johns Hopkins UniversityXinlei Chen - Johns Hopkins UniversityBrooke M Britton - Johns Hopkins UniversityDavid S Weiss - University of IowaJie Xiao - Johns Hopkins University
- Resource Type
- Journal article
- Publication Details
- Nature microbiology, Vol.10, pp.1521-1534
- DOI
- 10.1038/s41564-025-02011-w
- PMID
- 40425829
- PMCID
- PMC13032133
- NLM abbreviation
- Nat Microbiol
- ISSN
- 2058-5276
- eISSN
- 2058-5276
- Publisher
- NATURE PORTFOLIO
- Grant note
- NIH R01GM086447 and R35GM136436 (to J.X.), GM125656 (subcontract to J.X.), a Hamilton Smith Innovative Research Award (to J.X.): R01GM125656 NIHHamilton Smith Innovative Research Award
We thank all members of the Xiao lab for helpful discussions and feedback on the manuscript, and members of the Weiss lab for help with strain construction. We acknowledge the use of resources at the Protein and Crystallography Facility within the Carver College of Medicine at the University of Iowa along with advice and assistance from D. Reusch and N. Schnicker. Work in the Xiao lab was supported by NIH R01GM086447 and R35GM136436 (to J.X.), GM125656 (subcontract to J.X.), and a Hamilton Smith Innovative Research Award (to J.X.). Work in the Weiss lab was supported by NIH R01GM125656 (to D.S.W.).
- Language
- English
- Date published
- 05/27/2025
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984824177602771
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