ArticleJournal of bacteriology2013
Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- The lytic transglycosylase MltA participates in turnover of septal peptidoglycan inbioRxiv : the preprint server for biology · 2026Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- Comparative Study of Bacterial SPOR Domains Identifies Functionally Important Differences in Glycan Binding Affinity.Journal of bacteriology · 2022Article
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Stable inheritance of Sinorhizobium meliloti cell growth polarity requires an FtsN-like protein and an amidase.Nature communications · 2021Article
- Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division.Nature communications · 2019Article
- Disruption of divisome assembly rescued by FtsN-FtsA interaction inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.Journal of bacteriology · 2017Review
- The essential cell division protein FtsN contains a critical disulfide bond in a non-essential domain.Molecular microbiology · 2017Article
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- Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.Molecular microbiology · 2015Article
- Identification and Partial Characterization of Potential FtsL and FtsQ Homologs of Chlamydia.Frontiers in microbiology · 2015Article
- Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJ.Frontiers in microbiology · 2015Article
- Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Molecular & cellular proteomics : MCP · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
SPOR domains are about 75 amino acids long and probably bind septal peptidoglycan during cell division. We mutagenized 33 amino acids with surface-exposed side chains in the SPOR domain from an Escherichia coli cell division protein named FtsN. The mutant SPOR domains were fused to Tat-targeted green fluorescent protein ((TT)GFP) and tested for septal localization in live E. coli cells. Lesions at the following 5 residues reduced septal localization by a factor of 3 or more: Q251, S254, W283, R285, and I313. All of these residues map to a β-sheet in the published solution structure of FtsN(SPOR). Three of the mutant proteins (Q251E, S254E, and R285A mutants) were purified and found to be defective in binding to peptidoglycan sacculi in a cosedimentation assay. These results match closely with results from a previous study of the SPOR domain from DamX, even though these two SPOR domains share <20% amino acid identity. Taken together, these findings support the proposal that SPOR domains localize by binding to septal peptidoglycan and imply that the binding site is associated with the β-sheet. We also show that FtsN(SPOR) contains a disulfide bond between β-sheet residues C252 and C312. The disulfide bond contributes to protein stability, cell division, and peptidoglycan binding.
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