ArticleJournal of bacteriology2012
Role of a SpoVA protein in dipicolinic acid uptake into developing spores of Bacillus subtilis.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- Multiple independent losses of sporulation and peptidoglycan in theMicrobial genomics · 2024Article
- Visualization of SpoVAEa Protein Dynamics in Dormant Spores ofMicrobiology spectrum · 2022Article
- Effect of oxygen on the germination and culturability of Bacillus atrophaeus spores.International microbiology : the official journal of the Spanish Society for Microbiology · 2022Article
- The SpoVA membrane complex is required for dipicolinic acid import during sporulation and export during germination.Genes & development · 2022Article
- Mechanisms and Applications of Bacterial Sporulation and Germination in the Intestine.International journal of molecular sciences · 2022Review
- Antibacterial and Sporicidal Activity Evaluation of Theaflavin-3,3'-digallate.International journal of molecular sciences · 2022Article
- Clostridioides difficile spore germination: initiation to DPA release.Current opinion in microbiology · 2022Review
- Occurrence of genes encoding spore germination inMicrobial genomics · 2022Article
- Clostridioides difficile SpoVAD and SpoVAE Interact and Are Required for Dipicolinic Acid Uptake into Spores.Journal of bacteriology · 2021Article
- Structural, Metabolic and Evolutionary Comparison of Bacterial Endospore and Exospore Formation.Frontiers in microbiology · 2021Review
- Article
- Structural and functional analyses of the N-terminal domain of the A subunit of aProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The requirement for co-germinants during Clostridium difficile spore germination is influenced by mutations in yabG and cspA.PLoS pathogens · 2019Article
- Endophytic Paenibacillus amylolyticus KMCLE06 Extracted Dipicolinic Acid as Antibacterial Agent Derived via Dipicolinic Acid Synthetase Gene.Current microbiology · 2019Article
- Intracellular membranes of bacterial endospores are reservoirs for spore core membrane expansion during spore germination.Scientific reports · 2018Article
- Spore Heat Activation Requirements and Germination Responses Correlate with Sequences of Germinant Receptors and with the Presence of a SpecificApplied and environmental microbiology · 2017Article
- Genetic Characterization of the Exceptionally High Heat Resistance of the Non-toxic SurrogateFrontiers in microbiology · 2017Article
- A mobile genetic element profoundly increases heat resistance of bacterial spores.The ISME journal · 2016Article
- Characterization of Clostridium difficile Spores Lacking Either SpoVAC or Dipicolinic Acid Synthetase.Journal of bacteriology · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteins encoded by the spoVA operon, including SpoVAD, are essential for the uptake of the 1:1 chelate of pyridine-2,6-dicarboxylic acid (DPA(2,6)) and Ca(2+) into developing spores of the bacterium Bacillus subtilis. The crystal structure of B. subtilis SpoVAD has been determined recently, and a structural homology search revealed that SpoVAD shares significant structural similarity but not sequence homology to a group of enzymes that bind to and/or act on small aromatic molecules. We find that molecular docking placed DPA(2,6) exclusively in a highly conserved potential substrate-binding pocket in SpoVAD that is similar to that in the structurally homologous enzymes. We further demonstrate that SpoVAD binds both DPA(2,6) and Ca(2+)-DPA(2,6) with a similar affinity, while exhibiting markedly weaker binding to other DPA isomers. Importantly, mutations of conserved amino acid residues in the putative DPA(2,6)-binding pocket in SpoVAD essentially abolish its DPA(2,6)-binding capacity. Moreover, replacement of the wild-type spoVAD gene in B. subtilis with any of these spoVAD gene variants effectively eliminated DPA(2,6) uptake into developing spores in sporulation, although the variant proteins were still located in the spore inner membrane. Our results provide direct evidence that SpoVA proteins, in particular SpoVAD, are directly involved in DPA(2,6) movement into developing B. subtilis spores.
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