ArticleMolecular microbiology2017
Functional redundancy of division specific penicillin-binding proteins in Bacillus subtilis.
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 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- AEmerging microbes & infections · 2026Article
- Article
- Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division inJournal of bacteriology · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.PLoS genetics · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonicalbioRxiv : the preprint server for biology · 2025Article
- Localization and Single Molecule Dynamics ofCells · 2025Article
- Article
- Pbp4 provides transpeptidase activity to the FtsW-PbpB peptidoglycan synthase to drive cephalosporin resistance inAntimicrobial agents and chemotherapy · 2024Article
- Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile.Nature communications · 2023Article
- Recent Advances in Peptidoglycan Synthesis and Regulation in Bacteria.Biomolecules · 2023Review
- MraZ Transcriptionally Controls the Critical Level of FtsL Required for Focusing Z-Rings and Kickstarting Septation in Bacillus subtilis.Journal of bacteriology · 2022Article
- Article
- Live-Cell Profiling of Penicillin-Binding Protein Inhibitors inACS infectious diseases · 2022Article
- MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling.PLoS pathogens · 2022Article
- Genetic analysis of the septal peptidoglycan synthase FtsWI complex supports a conserved activation mechanism for SEDS-bPBP complexes.PLoS genetics · 2021Article
- Influence of core divisome proteins on cell division inMicrobiology (Reading, England) · 2021Article
- Population structure-guided profiling of antibiotic resistance patterns in clinicalEmerging microbes & infections · 2020Article
- Cell morphology maintenance in Bacillus subtilis through balanced peptidoglycan synthesis and hydrolysis.Scientific reports · 2020Article
- Review
- A regulatory pathway that selectively up-regulates elongasome function in the absence of class A PBPs.eLife · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial cell division involves the dynamic assembly of a diverse set of proteins that coordinate the invagination of the cell membrane and synthesis of cell wall material to create the new cell poles of the separated daughter cells. Penicillin-binding protein PBP 2B is a key cell division protein in Bacillus subtilis proposed to have a specific catalytic role in septal wall synthesis. Unexpectedly, we find that a catalytically inactive mutant of PBP 2B supports cell division, but in this background the normally dispensable PBP 3 becomes essential. Phenotypic analysis of pbpC mutants (encoding PBP 3) shows that PBP 2B has a crucial structural role in assembly of the division complex, independent of catalysis, and that its biochemical activity in septum formation can be provided by PBP 3. Bioinformatic analysis revealed a close sequence relationship between PBP 3 and Staphylococcus aureus PBP 2A, which is responsible for methicillin resistance. These findings suggest that mechanisms for rescuing cell division when the biochemical activity of PBP 2B is perturbed evolved prior to the clinical use of β-lactams.
Indexed as
Identifiers
What OpenQuestion holds
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.