ArticleMolecular microbiology2015
The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring.
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 49 papers.
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Who cites it
49 citing papers in PubMed.
- 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
- Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.Nature microbiology · 2022Article
- Activation of TnSmu1, an integrative and conjugative element, by an ImmR-like transcriptional regulator inMicrobiology (Reading, England) · 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
- Assembly dynamics of FtsZ and DamX during infection-related filamentation and division in uropathogenic E. coli.Nature communications · 2022Article
- In vitro reconstitution of Escherichia coli divisome activation.Nature communications · 2022Article
- The Longitudinal Dividing BacteriumInternational journal of molecular sciences · 2022Article
- The coiled-coil domain of Escherichia coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division.The Journal of biological chemistry · 2022Article
- FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The bacterial cell division protein fragmentThe Journal of biological chemistry · 2020Article
- Article
- DrpB (YedR) Is a Nonessential Cell Division Protein in Escherichia coli.Journal of bacteriology · 2020Article
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3 authors.
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Abstract
Assembly of the divisome in Escherichia coli occurs in two temporally distinct steps. First, FtsZ filaments attached to the membrane through interaction with FtsA and ZipA coalesce into a Z ring at midcell. Then, additional proteins are recruited to the Z ring in a hierarchical manner to form a complete divisome, activated by the arrival of FtsN. Recently, we proposed that the interaction of FtsA with itself competes with its ability to recruit downstream division proteins (both require the IC domain of FtsA) and ZipA's essential function is to promote the formation of FtsA monomers. Here, we tested whether overexpression of a downstream division protein could make ZipA dispensable, presumably by shifting the FtsA equilibrium to monomers. Only overexpression of FtsN bypassed ZipA and a conserved motif in the cytoplasmic domain of FtsN was required for both the bypass and interaction with FtsA. Also, this cytoplasmic motif had to be linked to the periplasmic E domain of FtsN to bypass ZipA, indicating that linkage of FtsA to periplasmic components of the divisome through FtsN was essential under these conditions. These results are used to further elaborate our model for the role of FtsA in recruiting downstream division proteins.
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