E. coliFtsN coordinates synthesis and degradation of septal peptidoglycan by partitioning between a synthesis track and a denuded glycan track Article Swipe
Zhixin Lyu
,
Xinxing Yang
,
Atsushi Yahashiri
,
Stephen Ha
,
Joshua W. McCausland
,
Xinlei Chen
,
Brooke M. Britton
,
David S. Weiss
,
Jie Xiao
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.05.13.594014
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.05.13.594014
The E. coli cell division protein FtsN was proposed to coordinate septal peptidoglycan (sPG) synthesis and degradation to ensure robust cell wall constriction without lethal lesions. Although the precise mechanism remains unclear, previous work highlights the importance of two FtsN domains: the E domain, which interacts with and activates the sPG synthesis complex FtsWIQLB, and the SPOR domain, which binds to denuded glycan (dnG) strands, key intermediates in sPG degradation. Here, we used single-molecule tracking of FtsN and FtsW (a proxy for the sPG synthesis complex FtsWIQLB) to investigate how FtsN coordinates the two opposing processes. We observed dynamic behaviors indicating that FtsN’s SPOR domain binds to dnGs cooperatively, which both sequesters the sPG synthesis complex on dnG (termed as the dnG-track) and protects dnGs from degradation by lytic transglycosylases (LTs). The release of the SPOR domain from dnGs leads to activating the sPG synthesis complex on the sPG-track and simultaneously exposing those same dnGs to degradation. Furthermore, FtsN’s SPOR domain self-interacts and facilitates the formation of a multimeric sPG synthesis complex on both tracks. The cooperative self-interaction of the SPOR domain creates a sensitive switch to regulate the partitioning of FtsN between the dnG- and sPG-tracks, thereby controlling the balance between sequestered and active populations of the sPG synthesis complex. As such, FtsN coordinates sPG synthesis and degradation in space and time.
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Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2024.05.13.594014
- https://www.biorxiv.org/content/biorxiv/early/2024/05/13/2024.05.13.594014.full.pdf
- OA Status
- green
- Cited By
- 2
- References
- 50
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4396901150
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4396901150Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2024.05.13.594014Digital Object Identifier
- Title
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E. coliFtsN coordinates synthesis and degradation of septal peptidoglycan by partitioning between a synthesis track and a denuded glycan trackWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2024Year of publication
- Publication date
-
2024-05-13Full publication date if available
- Authors
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Zhixin Lyu, Xinxing Yang, Atsushi Yahashiri, Stephen Ha, Joshua W. McCausland, Xinlei Chen, Brooke M. Britton, David S. Weiss, Jie XiaoList of authors in order
- Landing page
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https://doi.org/10.1101/2024.05.13.594014Publisher landing page
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https://www.biorxiv.org/content/biorxiv/early/2024/05/13/2024.05.13.594014.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2024/05/13/2024.05.13.594014.full.pdfDirect OA link when available
- Concepts
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Peptidoglycan, Chemistry, Glycan, Cytoplasm, Degradation (telecommunications), Biophysics, Cell biology, Biochemistry, Cell wall, Biology, Computer science, Glycoprotein, TelecommunicationsTop concepts (fields/topics) attached by OpenAlex
- Cited by
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2Total citation count in OpenAlex
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2025: 1, 2024: 1Per-year citation counts (last 5 years)
- References (count)
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50Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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