Journal article
FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli
Nature communications, Vol.13(1), pp.5751-5751
01/01/2022
DOI: 10.1038/s41467-022-33404-8
PMCID: PMC9525312
PMID: 36180460
Abstract
FtsN plays an essential role in promoting the inward synthesis of septal peptidoglycan (sPG) by the FtsWI complex during bacterial cell division. How it achieves this role is unclear. Here we use single-molecule tracking to investigate FtsN’s dynamics during sPG synthesis in E. coli. We show that septal FtsN molecules move processively at ~9 nm s−1, the same as FtsWI molecules engaged in sPG synthesis (termed sPG-track), but much slower than the ~30 nm s−1 speed of inactive FtsWI molecules coupled to FtsZ’s treadmilling dynamics (termed FtsZ-track). Importantly, processive movement of FtsN is exclusively coupled to sPG synthesis and is required to maintain active sPG synthesis by FtsWI. Our findings indicate that FtsN is part of the FtsWI sPG synthesis complex, and that while FtsN is often described as a “trigger” for the initiation for cell wall constriction, it must remain part of the processive FtsWI complex to maintain sPG synthesis activity. FtsN promotes the inward synthesis of septal peptidoglycan (sPG) through the FtsWI complex during bacterial cell division. Here, Lyu et al. apply single-molecule microscopy on E. coli to show that FtsN proteins (I) move processively at a speed similar to that of FtsWI molecules. (II) can be divided into two populations based on their speeds, and (III) their movement is driven exclusively by peptidoglycan synthesis
Details
- Title: Subtitle
- FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli
- Creators
- Zhixin Lyu - Johns Hopkins UniversityAtsushi Yahashiri - Roy J. and Lucille A. Carver College of MedicineXinxing Yang - Johns Hopkins UniversityJoshua W McCausland - Johns Hopkins UniversityGabriela M Kaus - Roy J. and Lucille A. Carver College of MedicineRyan McQuillen - Johns Hopkins UniversityDavid S Weiss - Roy J. and Lucille A. Carver College of MedicineJie Xiao - Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD, 21205, USA. xiao@jhmi.edu.
- Resource Type
- Journal article
- Publication Details
- Nature communications, Vol.13(1), pp.5751-5751
- DOI
- 10.1038/s41467-022-33404-8
- PMID
- 36180460
- PMCID
- PMC9525312
- NLM abbreviation
- Nat Commun
- eISSN
- 2041-1723
- Publisher
- Nature Publishing Group
- Grant note
- DOI: 10.13039/100000009, name: Foundation for the National Institutes of Health, award: R01GM086447, R35GM136436, GM125656, GM007445, R01GM125656, T32AI007511
- Language
- English
- Date published
- 01/01/2022
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984302217602771
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