ArticleProceedings of the National Academy of Sciences of the United States of America2015
Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 114 citations in OpenAlex.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Peptidoglycan Remodeling in Gram-Negative Bacteria: From Stress Adaptation to Antibiotic Tolerance and Therapeutic Targeting.Antibiotics (Basel, Switzerland) · 2026Review
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- The lytic transglycosylase MltA participates in turnover of septal peptidoglycan inbioRxiv : the preprint server for biology · 2026Article
- Functional characterization of the polar organizer protein FimV inJournal of bacteriology · 2026Article
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A novel peptidoglycan deacetylase modulates daughter cell separation in E. coli.PLoS genetics · 2025Article
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation inJournal of bacteriology · 2025Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Enterococcal cell wall remodelling underpins pathogenesis via the release of the Enteroccocal Polysaccharide Antigen (EPA).PLoS pathogens · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- Septal wall synthesis is sufficient to change ameba-like cells into uniform oval-shaped cells in Escherichia coli L-forms.Communications biology · 2024Article
- In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3Molecular microbiology · 2024Article
- Genetic requirements for uropathogenicmSystems · 2024Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Identification of a family of peptidoglycan transpeptidases reveals thatProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin A.International journal of biological macromolecules · 2024Article
- Integration of cell wall synthesis and chromosome segregation during cell division in Caulobacter.The Journal of cell biology · 2024Article
- Metagenomic analysis of hot spring soil for mining a novel thermostable enzybiotic.Applied microbiology and biotechnology · 2024Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial SPOR domains bind peptidoglycan (PG) and are thought to target proteins to the cell division site by binding to "denuded" glycan strands that lack stem peptides, but uncertainties remain, in part because septal-specific binding has yet to be studied in a purified system. Here we show that fusions of GFP to SPOR domains from the Escherichia coli cell-division proteins DamX, DedD, FtsN, and RlpA all localize to septal regions of purified PG sacculi obtained from E. coli and Bacillus subtilis. Treatment of sacculi with an amidase that removes stem peptides enhanced SPOR domain binding, whereas treatment with a lytic transglycosylase that removes denuded glycans reduced SPOR domain binding. These findings demonstrate unequivocally that SPOR domains localize by binding to septal PG, that the physiologically relevant binding site is indeed a denuded glycan, and that denuded glycans are enriched in septal PG rather than distributed uniformly around the sacculus. Accumulation of denuded glycans in the septal PG of both E. coli and B. subtilis, organisms separated by 1 billion years of evolution, suggests that sequential removal of stem peptides followed by degradation of the glycan backbone is an ancient feature of PG turnover during bacterial cell division. Linking SPOR domain localization to the abundance of a structure (denuded glycans) present only transiently during biogenesis of septal PG provides a mechanism for coordinating the function of SPOR domain proteins with the progress of cell division.
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