ArticleJournal of bacteriology2004
Bacillus subtilis StoA Is a thiol-disulfide oxidoreductase important for spore cortex synthesis.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- Distinct modes of cell division drivemBio · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Let There Be Light: Genome Reduction EnablesACS synthetic biology · 2023Article
- Diversity of CytochromeMicroorganisms · 2022Review
- Heme A Synthase Deficiency Affects the Ability ofInternational journal of molecular sciences · 2022Article
- Identification of Redox Partners of the Thiol-Disulfide Oxidoreductase SdbA in Streptococcus gordonii.Journal of bacteriology · 2019Article
- Bacillus megaterium adapts to acid stress condition through a network of genes: Insight from a genome-wide transcriptome analysis.Scientific reports · 2018Article
- Forespore Targeting of SpoVD in Bacillus subtilis Is Mediated by the N-Terminal Part of the Protein.Journal of bacteriology · 2018Article
- Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.BMC microbiology · 2015Article
- Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain.Frontiers in microbiology · 2015Article
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- An extended active-site motif controls the reactivity of the thioredoxin fold.The Journal of biological chemistry · 2014Article
- The two CcdA proteins of Bacillus anthracis differentially affect virulence gene expression and sporulation.Journal of bacteriology · 2013Article
- Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD.FEMS microbiology letters · 2013Article
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
- Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis.Molecular microbiology · 2012Article
- The physical state of water in bacterial spores.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus.Applied microbiology and biotechnology · 2009Review
- Homologues of the Bacillus subtilis SpoVB protein are involved in cell wall metabolism.Journal of bacteriology · 2009Article
- Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site.The Journal of biological chemistry · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus subtilis is an endospore-forming bacterium. There are indications that protein disulfide linkages occur in spores, but the role of thiol-disulfide chemistry in spore synthesis is not understood. Thiol-disulfide oxidoreductases catalyze formation or breakage of disulfide bonds in proteins. CcdA is the only B. subtilis thiol-disulfide oxidoreductase that has previously been shown to play some role in endospore biogenesis. In this work we show that lack of the StoA (YkvV) protein results in spores sensitive to heat, lysozyme, and chloroform. Compared to CcdA deficiency, StoA deficiency results in a 100-fold-stronger negative effect on sporulation efficiency. StoA is a membrane-bound protein with a predicted thioredoxin-like domain probably localized in the intermembrane space of the forespore. Electron microscopy of spores of CcdA- and StoA-deficient strains showed that the spore cortex is absent in both cases. The BdbD protein catalyzes formation of disulfide bonds in proteins on the outer side of the cytoplasmic membrane but is not required for sporulation. Inactivation of bdbD was found to suppress the sporulation defect of a strain deficient in StoA. Our results indicate that StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis.
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