ArticleNature communications2023
Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 19 citations in OpenAlex.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.Nature microbiology · 2026Article
- Uncovering an alternate pathway of antibiotic resistance in spore-forming bacteria.Nature communications · 2026Article
- A single DNA methylation site regulates cell fate during Clostridioides difficile sporulation.PLoS pathogens · 2026Article
- Carboxypeptidase activity drives L,D-transpeptidase essentiality during vegetative growth and sporulation inbioRxiv : the preprint server for biology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division inJournal of bacteriology · 2025Article
- Analysis of essential genes 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
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- Analysis of Essential Genes inbioRxiv : the preprint server for biology · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonicalbioRxiv : the preprint server for biology · 2025Article
- GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.Molecular biology of the cell · 2025Article
- Article
- Identification of a family of peptidoglycan transpeptidases reveals thatProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.PLoS pathogens · 2024Article
- Identification ofJournal of bacteriology · 2024Article
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4 authors at 2 institutions in 2 countries.
Funding
Abstract
The bacterial enzymes FtsW and FtsI, encoded in the highly conserved dcw gene cluster, are considered to be universally essential for the synthesis of septal peptidoglycan (PG) during cell division. Here, we show that the pathogen Clostridioides difficile lacks a canonical FtsW/FtsI pair, and its dcw-encoded PG synthases have undergone a specialization to fulfill sporulation-specific roles, including synthesizing septal PG during the sporulation-specific mode of cell division. Although these enzymes are directly regulated by canonical divisome components during this process, dcw-encoded PG synthases and their divisome regulators are dispensable for cell division during normal growth. Instead, C. difficile uses a bifunctional class A penicillin-binding protein as the core divisome PG synthase, revealing a previously unreported role for this class of enzymes. Our findings support that the emergence of endosporulation in the Firmicutes phylum facilitated the functional repurposing of cell division factors. Moreover, they indicate that C. difficile, and likely other clostridia, assemble a distinct divisome that therefore may represent a unique target for therapeutic interventions.
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