ArticlePloS one2010
Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 49 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
49 citing papers in PubMed.
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Article
- Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.Molecular diversity · 2024Review
- Identification of anti-Acta pharmaceutica Sinica. B · 2023Article
- An Arg/Ala-rich helix in the N-terminal region of M. tuberculosis FtsQ is a potential membrane anchor of the Z-ring.Communications biology · 2023Article
- Clostridioides difficile Phosphoproteomics Shows an Expansion of Phosphorylated Proteins in Stationary Growth Phase.mSphere · 2022Article
- Retraction: Novel Role of Phosphorylation-Dependent Interaction between FtsZ and FipA in Mycobacterial Cell Division.PloS one · 2022Article
- Heat Adaptation Induced Cross Protection Against Ethanol Stress inFrontiers in microbiology · 2021Article
- Rv0954 Is a Member of the Mycobacterial Cell Division Complex.Frontiers in microbiology · 2021Article
- Review
- PersistenteLife · 2019Article
- Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019Review
- The Dream of a Mycobacterium.Microbiology spectrum · 2019Review
- The Immune Escape Mechanisms ofInternational journal of molecular sciences · 2019Review
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions inmSphere · 2018Article
- The transpeptidase PbpA and noncanonical transglycosylase RodA ofThe Journal of biological chemistry · 2018Article
- Bacterial Cell Division: Nonmodels Poised to Take the Spotlight.Annual review of microbiology · 2017Review
- Epigenetic Phosphorylation Control of Mycobacterium tuberculosis Infection and Persistence.Microbiology spectrum · 2017Review
Corrections and comments
- Retraction · 2022-02-24Duplication of/in Image · Manipulation of Images · Original Data and/or Images not Provided and/or not Available · Unreliable Results and/or Conclusions ·
- Retracted
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the interrelationship between the products of the Mycobacterium tuberculosis gene cluster Rv0014c-Rv0019c, namely PknA (encoded by Rv0014c) and FtsZ-interacting protein A, FipA (encoded by Rv0019c) and the products of the division cell wall (dcw) cluster, namely FtsZ and FtsQ. M. smegmatis strains depleted in components of the two gene clusters have been complemented with orthologs of the respective genes of M. tuberculosis. Here we identify FipA as an interacting partner of FtsZ and FtsQ and establish that PknA-dependent phosphorylation of FipA on T77 and FtsZ on T343 is required for cell division under oxidative stress. A fipA knockout strain of M. smegmatis is less capable of withstanding oxidative stress than the wild type and showed elongation of cells due to a defect in septum formation. Localization of FtsQ, FtsZ and FipA at mid-cell was also compromised. Growth and survival defects under oxidative stress could be functionally complemented by fipA of M. tuberculosis but not its T77A mutant. Merodiploid strains of M. smegmatis expressing the FtsZ(T343A) showed inhibition of FtsZ-FipA interaction and Z ring formation under oxidative stress. Knockdown of FipA led to elongation of M. tuberculosis cells grown in macrophages and reduced intramacrophage growth. These data reveal a novel role of phosphorylation-dependent protein-protein interactions involving FipA, in the sustenance of mycobacterial cell division under oxidative stress.
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