A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilis

Elise Darmon, Ronald Dorenbos, Jochen Meens, Roland Freudl, Haike Antelmann, Michael Hecker, Oscar P. Kuipers, Sierd Bron, Wim J. Quax, Jean-Yves F. Dubois, Jan Maarten van Dijl*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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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.

Original languageEnglish
Pages (from-to)6876-6885
Number of pages10
JournalApplied and environmental microbiology
Volume72
Issue number11
DOIs
Publication statusPublished - Nov-2006

Keywords

  • STAPHYLOCOCCUS-HYICUS LIPASE
  • GRAM-POSITIVE BACTERIA
  • PROTEIN SECRETION
  • ESCHERICHIA-COLI
  • 2-COMPONENT SYSTEM
  • ALPHA-AMYLASE
  • PEPTIDE
  • OXIDOREDUCTASES
  • MEMBRANE
  • ROLES

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