ArticleJournal of bacteriology2012
ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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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.
The trial behind it
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Who cites it
42 citing papers in PubMed, 67 citations in OpenAlex.
- The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.Nature microbiology · 2026Article
- Molecular Cytology of 'Little Animals': Personal Recollections ofLife (Basel, Switzerland) · 2023Review
- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- Organization of peptidoglycan synthesis in nodes and separate rings at different stages of cell division of Streptococcus pneumoniae.Molecular microbiology · 2021Article
- Elongation at Midcell in Preparation of Cell Division Requires FtsZ, but Not MreB nor PBP2 inFrontiers in microbiology · 2021Article
- Article
- Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Journal of bacteriology · 2020Article
- Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ.Scientific reports · 2019Article
- Lytic transglycosylases RlpA and MltC assist in Vibrio cholerae daughter cell separation.Molecular microbiology · 2019Article
- Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division.Nature communications · 2018Article
- Outer membrane lipoprotein RlpA is a novel periplasmic interaction partner of the cell division protein FtsK in Escherichia coli.Scientific reports · 2018Article
- YtfB, an OapA Domain-Containing Protein, Is a New Cell Division Protein in Escherichia coli.Journal of bacteriology · 2018Article
- Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.The Journal of biological chemistry · 2017Article
- Determinants of Bacterial Morphology: From Fundamentals to Possibilities for Antimicrobial Targeting.Frontiers in microbiology · 2017Review
- Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- A Mutant Isoform of ObgE Causes Cell Death by Interfering with Cell Division.Frontiers in microbiology · 2017Article
- A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus.Molecular microbiology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rod-shaped bacteria grow by a repetitive cycle of elongation followed by division, and the mechanisms responsible for these two processes have been studied for decades. However, little is known about what happens during the transition between the two activities. At least one event occurs after elongation ends and before division commences, that being the insertion of new cell wall peptidoglycan into a narrowly circumscribed ribbon around midcell where septation is destined to take place. This insertion does not depend on the presence of the septation-specific protein PBP3 and is therefore known as PBP3-independent peptidoglycan synthesis (PIPS). Here we report that only FtsZ and ZipA are required to generate PIPS in wild-type Escherichia coli. PIPS does not require the participation of other members of the divisome, the MreB-directed cell wall elongation complex, alternate peptidoglycan synthases, the major peptidoglycan amidases, or any of the low-molecular-weight penicillin binding proteins. ZipA-directed PIPS may represent an intermediate stage that connects cell wall elongation to septal invagination and may be the reason ZipA is essential in the gammaproteobacteria.
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Registered trials
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.