ArticleMolecular microbiology2015
A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling.
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 28 papers.
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Who cites it
28 citing papers in PubMed.
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Anchors: A way for FtsZ filaments to stay membrane bound.Molecular microbiology · 2023Review
- Chiral and nematic phases of flexible active filaments.Nature physics · 2023Article
- The Longitudinal Dividing BacteriumInternational journal of molecular sciences · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Bacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitment.Journal of bacteriology · 2020Article
- Overproduction of a Dominant Mutant of the Conserved Era GTPase Inhibits Cell Division in Escherichia coli.Journal of bacteriology · 2020Article
- Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Journal of bacteriology · 2020Article
- High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.Acta crystallographica. Section F, Structural biology communications · 2020Article
- At the Heart of Bacterial Cytokinesis: The Z Ring.Trends in microbiology · 2019Review
- An Essential Regulator of Bacterial Division Links FtsZ to Cell Wall Synthase Activation.Current biology : CB · 2019Article
- Gain-of-function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling.Molecular microbiology · 2018Article
- Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.mBio · 2018Article
- Article
- Suppression of a ThermosensitiveJournal of bacteriology · 2018Article
- Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division.F1000Research · 2018Review
- CbtA toxin of Escherichia coli inhibits cell division and cell elongation via direct and independent interactions with FtsZ and MreB.PLoS genetics · 2017Article
- Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.Nature communications · 2017Article
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3 authors.
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Abstract
The earliest step in Escherichia coli cell division consists of the assembly of FtsZ protein into a proto-ring structure, tethered to the cytoplasmic membrane by FtsA and ZipA. The proto-ring then recruits additional cell division proteins to form the divisome. Previously we described an ftsZ allele, ftsZL169R , which maps to the side of the FtsZ subunit and confers resistance to FtsZ assembly inhibitory factors including Kil of bacteriophage λ. Here we further characterize this allele and its mechanism of resistance. We found that FtsZL169R permits the bypass of the normally essential ZipA, a property previously observed for FtsA gain-of-function mutants such as FtsA* or increased levels of the FtsA-interacting protein FtsN. Similar to FtsA*, FtsZL169R also can partially suppress thermosensitive mutants of ftsQ or ftsK, which encode additional divisome proteins, and confers strong resistance to excess levels of FtsA, which normally inhibit FtsZ ring function. Additional genetic and biochemical assays provide further evidence that FtsZL169R enhances FtsZ protofilament bundling, thereby conferring resistance to assembly inhibitors and bypassing the normal requirement for ZipA. This work highlights the importance of FtsZ protofilament bundling during cell division and its likely role in regulating additional divisome activities.
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