ArticleMolecular microbiology2017
The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain.
Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Disulfide bonds are required for cell division, cell envelope biogenesis and antibiotic resistance proteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Comparative Study of Bacterial SPOR Domains Identifies Functionally Important Differences in Glycan Binding Affinity.Journal of bacteriology · 2022Article
- Stable inheritance of Sinorhizobium meliloti cell growth polarity requires an FtsN-like protein and an amidase.Nature communications · 2021Article
- How the assembly and protection of the bacterial cell envelope depend on cysteine residues.The Journal of biological chemistry · 2020Review
- Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes.Molecular microbiology · 2019Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.Journal of bacteriology · 2018Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli.Journal of bacteriology · 2017Article
- The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.Journal of bacteriology · 2017Review
- Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.The Journal of biological chemistry · 2017Article
- Absence of Thiol-Disulfide Oxidoreductase DsbA ImpairsFrontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Disulfide bonds are found in many proteins associated with the cell wall of Escherichia coli, and for some of these proteins the disulfide bond is critical to their stability and function. One protein found to contain a disulfide bond is the essential cell division protein FtsN, but the importance of this bond to the protein's structural integrity is unclear. While it evidently plays a role in the proper folding of the SPOR domain of FtsN, this domain is non-essential, suggesting that the disulfide bond might also be dispensable. However, we find that FtsN mutants lacking cysteines give rise to filamentous growth. Furthermore, FtsN protein levels in strains expressing these mutants were significantly lower than in a strain expressing the wild-type allele, as were FtsN levels in strains incapable of making disulfide bonds (dsb
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Registered trials
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