ArticleApplied and environmental microbiology2006
A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilis.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 30 citations in OpenAlex.
- The phosphate specific transport system protein PhoU modulates persister cell formation of Klebsiella pneumoniae.Molecular genetics and genomics : MGG · 2026Article
- Exploration of Length and Hydrophobicity Requirements for Optimal α-Amylase Secretion in Bacillus subtilis Based on Rational Design.Microbial biotechnology · 2026Article
- Impact of expression systems on the transcriptome ofApplied and environmental microbiology · 2025Article
- Toward Antibody Production in Genome-MinimizedACS synthetic biology · 2025Article
- Let There Be Light: Genome Reduction EnablesACS synthetic biology · 2023Article
- A secretion biosensor for monitoring Sec-dependent protein export in Corynebacterium glutamicum.Microbial cell factories · 2020Article
- Mutation of the Thiol-Disulfide Oxidoreductase SdbA Activates the CiaRH Two-Component System, Leading to Bacteriocin Expression Shutdown in Streptococcus gordonii.Journal of bacteriology · 2016Article
- Disulfide Bonds of Proteins Displayed on Spores of Bacillus subtilis Can Occur Spontaneously.Current microbiology · 2015Article
- Small regulatory RNA-induced growth rate heterogeneity of Bacillus subtilis.PLoS genetics · 2015Article
- The multidrug ABC transporter BmrC/BmrD of Bacillus subtilis is regulated via a ribosome-mediated transcriptional attenuation mechanism.Nucleic acids research · 2014Article
- Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.Applied and environmental microbiology · 2014Article
- Bacillus subtilis: from soil bacterium to super-secreting cell factory.Microbial cell factories · 2013Article
- Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Applied and environmental microbiology · 2012Article
- Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.PloS one · 2011Article
- Contributions of the pre- and pro-regions of a Staphylococcus hyicus lipase to secretion of a heterologous protein by Bacillus subtilis.Applied and environmental microbiology · 2010Article
- The large mechanosensitive channel MscL determines bacterial susceptibility to the bacteriocin sublancin 168.Antimicrobial agents and chemotherapy · 2009Article
- Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus.Applied microbiology and biotechnology · 2009Review
- Immunity to the bacteriocin sublancin 168 Is determined by the SunI (YolF) protein of Bacillus subtilis.Antimicrobial agents and chemotherapy · 2009Article
- The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.Applied and environmental microbiology · 2008Article
- Modulation of thiol-disulfide oxidoreductases for increased production of disulfide-bond-containing proteins in Bacillus subtilis.Applied and environmental microbiology · 2008Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gram-positive bacterium Bacillus subtilis secretes high levels of proteins into its environment. Most of these secretory proteins are exported from the cytoplasm in an unfolded state and have to fold efficiently after membrane translocation. As previously shown for alpha-amylases of Bacillus species, inefficient posttranslocational protein folding is potentially detrimental and stressful. In B. subtilis, this so-called secretion stress is sensed and combated by the CssRS two-component system. Two known members of the CssRS regulon are the htrA and htrB genes, encoding potential extracytoplasmic chaperone proteases for protein quality control. In the present study, we investigated whether high-level production of a secretory protein with two disulfide bonds, PhoA of Escherichia coli, induces secretion stress in B. subtilis. Our results show that E. coli PhoA production triggers a relatively moderate CssRS-dependent secretion stress response in B. subtilis. The intensity of this response is significantly increased in the absence of BdbC, which is a major determinant for posttranslocational folding of disulfide bond-containing proteins in B. subtilis. Our findings show that BdbC is required to limit the PhoA-induced secretion stress. This conclusion focuses interest on the BdbC-dependent folding pathway for biotechnological production of proteins with disulfide bonds in B. subtilis and related bacilli.
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