ArticleMolecular microbiology2014
A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface.
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 21 papers.
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Who cites it
21 citing papers in PubMed.
- Article
- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- 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
- Nucleotide-dependent activities of FtsA regulate the early establishment of a functional divisome during theFrontiers in microbiology · 2023Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- 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
- Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Journal of bacteriology · 2020Article
- Direct Interaction between the Two Z Ring Membrane Anchors FtsA and ZipA.Journal of bacteriology · 2019Article
- Gain-of-function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling.Molecular microbiology · 2018Article
- FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.Molecular microbiology · 2018Article
- Comprehensive analysis of central carbon metabolism illuminates connections between nutrient availability, growth rate, and cell morphology in Escherichia coli.PLoS genetics · 2018Article
- Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division.F1000Research · 2018Review
- Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.Nature communications · 2017Article
- Assembly and activation of the Escherichia coli divisome.Molecular microbiology · 2017Review
- Splitsville: structural and functional insights into the dynamic bacterial Z ring.Nature reviews. Microbiology · 2016Review
- 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.Molecular microbiology · 2015Article
- Guiding divisome assembly and controlling its activity.Current opinion in microbiology · 2015Review
Corrections and comments
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Authors and funding
3 authors.
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Abstract
In Escherichia coli, initial assembly of the Z ring for cell division requires FtsZ plus the essential Z ring-associated proteins FtsA and ZipA. Thermosensitive mutations in ftsA, such as ftsA27, map in or near its ATP binding pocket and result in cell division arrest at non-permissive temperatures. We found that purified wild-type FtsA bound and hydrolysed ATP, whereas FtsA27 was defective in both activities. FtsA27 was also less able to localize to the Z ring in vivo. To investigate the role of ATP transactions in FtsA function in vivo, we isolated intragenic suppressors of ftsA27. Suppressor lesions in the ATP site restored the ability of FtsA27 to compete with ZipA at the Z ring, and enhanced ATP binding and hydrolysis in vitro. Notably, suppressors outside of the ATP binding site, including some mapping to the FtsA-FtsA subunit interface, also enhanced ATP transactions and exhibited gain of function phenotypes in vivo. These results suggest that allosteric effects, including changes in oligomeric state, may influence the ability of FtsA to bind and/or hydrolyse ATP.
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