A Disulfide Bond-Containing Alkaline Phosphatase Triggers a BdbC-Dependent Secretion Stress Response in Bacillus subtilis
| Autor: | Michael Hecker, Wim J. Quax, Sierd Bron, Ronald Dorenbos, Elise Darmon, Jan Maarten van Dijl, Haike Antelmann, Roland Freudl, Jean-Yves F. Dubois, Oscar P. Kuipers, Jochen Meens |
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| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Molecular Genetics, Cell Biochemistry, Faculty of Science and Engineering, Translational Immunology Groningen (TRIGR), Biopharmaceuticals, Discovery, Design and Delivery (BDDD), Nanotechnology and Biophysics in Medicine (NANOBIOMED) |
| Rok vydání: | 2006 |
| Předmět: |
Proteomics
Protein Folding ALPHA-AMYLASE 2-COMPONENT SYSTEM Bacillus subtilis genetics [Serine Endopeptidases] medicine.disease_cause Applied Microbiology and Biotechnology PEPTIDE enzymology [Bacillus subtilis] ROLES Ecology biology Escherichia coli Proteins Serine Endopeptidases OXIDOREDUCTASES metabolism [Bacillus subtilis] secretion [Protein Disulfide Reductase (Glutathione)] Biochemistry ESCHERICHIA-COLI physiology [Bacillus subtilis] Protein folding chemistry [Alkaline Phosphatase] genetics [Bacterial Proteins] Biotechnology PROTEIN SECRETION GRAM-POSITIVE BACTERIA metabolism [Bacterial Proteins] Genetics and Molecular Biology Protein-disulfide reductase (glutathione) metabolism [Alkaline Phosphatase] phoA protein E coli Bacterial Proteins YkdA protein Bacillus subtilis ddc:570 metabolism [Serine Endopeptidases] medicine secretion [Bacterial Proteins] methods [Biotechnology] Secretion Escherichia coli BdbC protein Bacillus subtilis Protein Disulfide Reductase (Glutathione) Gene Expression Regulation Bacterial Alkaline Phosphatase biology.organism_classification YvtA protein Bacillus subtilis Secretory protein Regulon STAPHYLOCOCCUS-HYICUS LIPASE Chaperone (protein) Mutation biology.protein bacteria genetics [Alkaline Phosphatase] genetics [Bacillus subtilis] MEMBRANE Heat-Shock Response Food Science |
| Zdroj: | Applied and environmental microbiology, 72(11), 6876-6885. AMER SOC MICROBIOLOGY Applied and environmental microbiology 72, 6876-6885 (2006). doi:10.1128/AEM.01176-06 |
| ISSN: | 1098-5336 0099-2240 |
| DOI: | 10.1128/aem.01176-06 |
| Popis: | 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 α-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. |
| Databáze: | OpenAIRE |
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