ArticleThe EMBO journal1999
ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
92 citing papers in PubMed, 182 citations in OpenAlex.
- PA5402-5407 of Pseudomonas aeruginosa Regulate the Expression of the Aa3-Type Oxidases and Their Growth Under Carbon Starvation and High-Density Conditions.Current microbiology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Anchors: A way for FtsZ filaments to stay membrane bound.Molecular microbiology · 2023Review
- SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.Nature communications · 2023Article
- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- A Novel Z-Ring Associated Protein ZapA-Like Protein (PA5407) FromFrontiers in microbiology · 2021Article
- Assembly properties of bacterial tubulin homolog FtsZ regulated by the positive regulator protein ZipA and ZapA from Pseudomonas aeruginosa.Scientific reports · 2020Article
- A stochastic model for dynamics of FtsZ filaments and the formation of Z -ring.The European physical journal. E, Soft matter · 2020Article
- Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Journal of bacteriology · 2020Article
- Transient Membrane-Linked FtsZ Assemblies Precede Z-Ring Formation in Escherichia coli.Current biology : CB · 2020Article
- Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ.Scientific reports · 2019Article
- Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division.Nature communications · 2018Article
- 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
- Sporulation-specific cell division defects in ylmE mutants of Streptomyces coelicolor are rescued by additional deletion of ylmD.Scientific reports · 2018Article
- Suppression of a ThermosensitiveJournal of bacteriology · 2018Article
- ZipA and FtsA* stabilize FtsZ-GDP miniring structures.Scientific reports · 2017Article
- The hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.PloS one · 2017Article
- SepG coordinates sporulation-specific cell division and nucleoid organization in Streptomyces coelicolor.Open biology · 2016Article
32 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
The first visible event in prokaryotic cell division is the assembly of the soluble, tubulin-like FtsZ GTPase into a membrane-associated cytokinetic ring that defines the division plane in bacterial and archaeal cells. In the temperature-sensitive ftsZ84 mutant of Escherichia coli, this ring assembly is impaired at the restrictive temperature causing lethal cell filamentation. Here I present genetic and morphological evidence that a 2-fold higher dosage of the division gene zipA suppresses thermosensitivity of the ftsZ84 mutant by stabilizing the labile FtsZ84 ring structure in vivo. I demonstrate that purified ZipA promotes and stabilizes protofilament assembly of both FtsZ and FtsZ84 in vitro and cosediments with the protofilaments. Furthermore, ZipA organizes FtsZ protofilaments into arrays of long bundles or sheets that probably represent the physiological organization of the FtsZ ring in bacterial cells. The N-terminal cytoplasmic domain of membrane-anchored ZipA contains sequence elements that resemble the microtubule-binding signature motifs in eukaryotic Tau, MAP2 and MAP4 proteins. It is postulated that the MAP-Tau-homologous motifs in ZipA mediate its binding to FtsZ, and that FtsZ-ZipA interaction represents an ancient prototype of the protein-protein interaction that enables MAPs to suppress microtubule catastrophe and/or to promote rescue.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.