ArticleJournal of molecular biology2010
Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- Uncovering an alternate pathway of antibiotic resistance in spore-forming bacteria.Nature communications · 2026Article
- Toad's survivability and soil microbiome alterations impacted via individual abundance.Biologia futura · 2025Article
- RagB stimulates the activity of the peptidoglycan polymerase RodA in Bacillus subtilis.EMBO reports · 2025Article
- Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile.Nature communications · 2023Article
- Bacterial cell surface nanoenvironment requires a specialized chaperone to activate a peptidoglycan biosynthetic enzyme.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.Nature communications · 2023Article
- A cortex-specific penicillin-binding protein contributes to heat resistance in Clostridioides difficile spores.Anaerobe · 2021Article
- Interactions ofMicroorganisms · 2021Article
- A dynamic, ring-forming MucB / RseB-like protein influences spore shape in Bacillus subtilis.PLoS genetics · 2020Article
- Uncovering Unappreciated Activities and Niche Functions of Bacterial Cell Wall Enzymes.Current biology : CB · 2020Review
- The PASTA domains ofMicrobiology (Reading, England) · 2020Article
- A PopZ-linked apical recruitment assay for studying protein-protein interactions in the bacterial cell envelope.Molecular microbiology · 2019Article
- Chemical tools to characterize peptidoglycan synthases.Current opinion in chemical biology · 2019Review
- Interactions Screenings Unearth Potential New Divisome Components in theMicroorganisms · 2019Article
- A LysM Domain Intervenes in Sequential Protein-Protein and Protein-Peptidoglycan Interactions Important for Spore Coat Assembly inJournal of bacteriology · 2019Article
- A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery.PLoS genetics · 2018Article
- Forespore Targeting of SpoVD in Bacillus subtilis Is Mediated by the N-Terminal Part of the Protein.Journal of bacteriology · 2018Article
- RodA as the missing glycosyltransferase in Bacillus subtilis and antibiotic discovery for the peptidoglycan polymerase pathway.Nature microbiology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The requirement of peptidoglycan synthesis for growth complicates the analysis of interactions between proteins involved in this pathway. In particular, the latter steps that involve membrane-linked substrates have proven largely recalcitrant to in vivo analysis. Here, we have taken advantage of the peptidoglycan synthesis that occurs during sporulation in Bacillus subtilis to examine the interactions between SpoVE, a nonessential, sporulation-specific homolog of the well-conserved and essential SEDS (shape elongation, division, and sporulation) proteins, and SpoVD, a nonessential class B penicillin binding protein. We found that localization of SpoVD is dependent on SpoVE and that SpoVD protects SpoVE from in vivo proteolysis. Co-immunoprecipitations and fluorescence resonance energy transfer experiments indicated that SpoVE and SpoVD interact, and co-affinity purification in Escherichia coli demonstrated that this interaction is direct. Finally, we generated a functional protein consisting of an SpoVE-SpoVD fusion and found that a loss-of-function point mutation in either part of the fusion resulted in loss of function of the entire fusion that was not complemented by a wild-type protein. Thus, SpoVE has a direct and functional interaction with SpoVD, and this conclusion will facilitate understanding the essential function that SpoVE and related SEDS proteins, such as FtsW and RodA, play in bacterial growth and division.
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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.