ArticleMolecular microbiology2014
A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- The transcription factor Vca0578 (DsvR) mediated expression of ZapC is required to promote cell division during lytic transglycosylase insufficiency inbioRxiv : the preprint server for biology · 2026Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.Nature communications · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- Spatio-temporal organization of theEcoSal Plus · 2024Review
- Septal wall synthesis is sufficient to change ameba-like cells into uniform oval-shaped cells in Escherichia coli L-forms.Communications biology · 2024Article
- Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Plasticity in the cell division processes of obligate intracellular bacteria.Frontiers in cellular and infection microbiology · 2023Review
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.Nature microbiology · 2022Article
- Cell wall synthesis and remodelling dynamics determine division site architecture and cell shape in Escherichia coli.Nature microbiology · 2022Article
- FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.Nature communications · 2022Article
- Comparative Study of Bacterial SPOR Domains Identifies Functionally Important Differences in Glycan Binding Affinity.Journal of bacteriology · 2022Article
- Article
- In vitro reconstitution of Escherichia coli divisome activation.Nature communications · 2022Article
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- Coupling between DNA replication, segregation, and the onset of constriction in Escherichia coli.Cell reports · 2022Article
- TheInternational journal of molecular sciences · 2021Article
- Stable inheritance of Sinorhizobium meliloti cell growth polarity requires an FtsN-like protein and an amidase.Nature communications · 2021Article
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2 authors.
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Abstract
FtsN is a bitopic membrane protein and the last essential component to localize to the Escherichia coli cell division machinery, or divisome. The periplasmic SPOR domain of FtsN was previously shown to localize to the divisome in a self-enhancing manner, relying on the essential activity of FtsN and the peptidoglycan synthesis and degradation activities of FtsI and amidases respectively. Because FtsN has a known role in recruiting amidases and is predicted to stimulate the activity of FtsI, it follows that FtsN initially localizes to division sites in a SPOR-independent manner. Here, we show that the cytoplasmic and transmembrane domains of FtsN (FtsN(Cyto - TM)) facilitated localization of FtsN independently of its SPOR domain but dependent on the early cell division protein FtsA. In addition, SPOR-independent localization preceded SPOR-dependent localization, providing a mechanism for the initial localization of FtsN. In support of the role of FtsNCyto - TM in FtsN function, a variant of FtsN lacking the cytoplasmic domain localized to the divisome but failed to complement an ftsN deletion unless it was overproduced. Simultaneous removal of the cytoplasmic and SPOR domains abolished localization and complementation. These data support a model in which FtsA-FtsN interaction recruits FtsN to the divisome, where it can then stimulate the peptidoglycan remodelling activities required for SPOR-dependent localization.
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