ArticleMolecular microbiology2015
Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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122 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- RodZ acts through MreBCD to activate the elongasome inJournal of bacteriology · 2026Article
- Altered regulation of septal peptidoglycan synthesis modulates β-lactam susceptibility in Pseudomonas aeruginosa.PLoS genetics · 2026Article
- The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.Nature microbiology · 2026Article
- FtsW protein-protein interactions visualized in live Staphylococcus aureus cells by FLIM-FRET.Nature communications · 2026Article
- The lytic transglycosylase MltA participates in turnover of septal peptidoglycan inbioRxiv : the preprint server for biology · 2026Article
- Control of cell division by anbioRxiv : the preprint server for biology · 2026Article
- Optimizing spatial organization of FtsZ rings for large-scale constriction in synthetic cells.Nature communications · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.PLoS genetics · 2025Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- Septal wall synthesis is sufficient to change ameba-like cells into uniform oval-shaped cells in Escherichia coli L-forms.Communications biology · 2024Article
- Determining the rate-limiting processes for cell division in Escherichia coli.Nature communications · 2024Article
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- The Influence of Exogenous CdS Nanoparticles on the Growth and Carbon Assimilation Efficiency ofBiology · 2024Article
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- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
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62 more citing papers are in PubMed but not listed here.
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4 authors.
Funding
Abstract
Escherichia coli FtsN is a bitopic membrane protein that is essential for triggering active cell constriction. A small periplasmic subdomain ((E) FtsN) is required and sufficient for function, but its mechanism of action is unclear. We isolated extragenic (E) FtsN*-suppressing mutations that restore division in cells producing otherwise non-functional variants of FtsN. These mapped to the IC domain of FtsA in the cytoplasm and to small subdomains of the FtsB and FtsL proteins in the periplasm. All FtsB and FtsL variants allowed survival without (E) FtsN, but many then imposed a new requirement for interaction between the cytoplasmic domain of FtsN ((N) FtsN) and FtsA. Alternatively, variants of FtsA, FtsB or FtsL acted synergistically to allow cell division in the complete absence of FtsN. Strikingly, moreover, substitution of a single residue in FtsB (E56) proved sufficient to rescue ΔftsN cells as well. In FtsN(+) cells, (E) FtsN*-suppressing mutations promoted cell fission at an abnormally small cell size, and caused cell shape and integrity defects under certain conditions. This and additional evidence support a model in which FtsN acts on either side of the membrane to induce a conformational switch in both FtsA and the FtsBLQ subcomplex to de-repress septal peptidoglycan synthesis and membrane invagination.
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