ArticleJournal of bacteriology2006
FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli.
Article in Journal of bacteriology, 2006. 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.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Functional Characterization of the Cell Division Gene Cluster of the Wall-less BacteriumFrontiers in microbiology · 2021Article
- Article
- Turgor Pressure and Possible Constriction Mechanisms in Bacterial Division.Frontiers in microbiology · 2018Review
- ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli.Scientific reports · 2017Article
- Whole genome re-sequencing to identify suppressor mutations of mutant and foreign Escherichia coli FtsZ.PloS one · 2017Article
- Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.Journal of bacteriology · 2017Article
- Membrane remodelling in bacteria.Journal of structural biology · 2016Review
- FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.Biochemistry · 2016Article
- Potential Molecular Targets for Narrow-Spectrum Agents to Combat Mycoplasma pneumoniae Infection and Disease.Frontiers in microbiology · 2016Review
- Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division.eLife · 2014Article
- The FtsZ-like protein FtsZm of Magnetospirillum gryphiswaldense likely interacts with its generic homolog and is required for biomineralization under nitrate deprivation.Journal of bacteriology · 2014Article
- Chrysophaentins are competitive inhibitors of FtsZ and inhibit Z-ring formation in live bacteria.Bioorganic & medicinal chemistry · 2013Article
- The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.Molecular microbiology · 2013Article
- Bacterial cytokinesis: From Z ring to divisome.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.The Journal of biological chemistry · 2012Article
- Inside-out Z rings--constriction with and without GTP hydrolysis.Molecular microbiology · 2011Article
- FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Microbiology and molecular biology reviews : MMBR · 2010Review
- Kinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesis.PLoS computational biology · 2008Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
FtsZs from Mycoplasma pulmonis (MpuFtsZ) and Bacillus subtilis (BsFtsZ) are only 46% and 53% identical in amino acid sequence to FtsZ from Escherichia coli (EcFtsZ). In the present study we show that MpuFtsZ and BsFtsZ can function for cell division in E. coli provided we make two modifications. First, we replaced their C-terminal tails with that from E. coli, giving the foreign FtsZ the binding site for E. coli FtsA and ZipA. Second, we selected for mutations in the E. coli genome that facilitated division by the foreign FtsZs. These suppressor strains arose at a relatively high frequency of 10(-3) to 10(-5), suggesting that they involve loss-of-function mutations in multigene pathways. These pathways may be negative regulators of FtsZ or structural pathways that facilitate division by slightly defective FtsZ. Related suppressor strains were obtained for EcFtsZ containing certain point mutations or insertions of yellow fluorescent protein. The ability of highly divergent FtsZs to function for division in E. coli is consistent with a two-part mechanism. FtsZ assembles the Z ring, and perhaps generates the constriction force, through self interactions; the downstream division proteins remodel the peptidoglycan wall by interacting with each other and the wall. The C-terminal peptide of FtsZ, which binds FtsA, provides the link between FtsZ assembly and peptidoglycan remodeling.
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