ArticleJournal of bacteriology2025
Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division in
Article in Journal of bacteriology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Uncovering an alternate pathway of antibiotic resistance in spore-forming bacteria.Nature communications · 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
- Analysis of essential genes inJournal of bacteriology · 2025Article
- 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
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Abstract
Peptidoglycan synthesis is an essential driver of bacterial growth and division. The final steps of this crucial process involve the polymerization of glycan strands by shape, elongation, division, and sporulation (SEDS) family glycosyltransferases and the cross-linking of peptide cross-bridges by class B penicillin-binding proteins (bPBP). While many bacteria use distinct bPBPs to perform specialized roles during a given cellular process, some bPBPs can play redundant roles, particularly in the presence of certain cell wall stresses. Our understanding of these compensatory mechanisms, however, remains incomplete. Endospore-forming bacteria typically encode multiple bPBPs to drive morphological changes required for sporulation. The sporulation-specific bPBP, SpoVD, synthesizes the polar division septum and the cortex peptidoglycan layer during sporulation in the pathogen
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