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Applied and Environmental Microbiology, November 2006, p. 6876-6885, Vol. 72, No. 11
0099-2240/06/$08.00+0     doi:10.1128/AEM.01176-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Disulfide Bond-Containing Alkaline Phosphatase Triggers a BdbC-Dependent Secretion Stress Response in Bacillus subtilis

Elise Darmon ,1,{dagger},{ddagger} Ronald Dorenbos,2,{dagger},§ Jochen Meens,3,¶ Roland Freudl,3 Haike Antelmann,4 Michael Hecker,4 Oscar P. Kuipers,1 Sierd Bron,1 Wim J. Quax,2 Jean-Yves F. Dubois,2,5 and Jan Maarten van Dijl2,5*

Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands,1 Department of Pharmaceutical Biology, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands,2 Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany,3 Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt- Universität Greifswald, D-17487 Greifswald, Germany,4 Laboratory of Molecular Bacteriology, Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Hanzeplein 1, P.O. Box 30001, 9700 RB Groningen, The Netherlands5

Received 21 May 2006/ Accepted 6 August 2006

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.

* Corresponding author. Mailing address: Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Hanzeplein 1, P.O. Box 30001, 9700 RB Groningen, The Netherlands. Phone: 31 50 3633079. Fax: 31 50 363 3528. E-mail: J.M.van.Dijl{at}med.umcg.nl.

{dagger} E.D. and R.D. contributed equally to this work.

{ddagger} Present address: Institute of Cell and Molecular Biology, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, United Kingdom.

§ Present address: Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115.

Present address: Zentrum für Infektionsmedizin, Institut für Mikrobiologie, Tierärztliche Hochschule Hannover, Bischofsholer Damm 15, 30173 Hannover, Germany.

Applied and Environmental Microbiology, November 2006, p. 6876-6885, Vol. 72, No. 11
0099-2240/06/$08.00+0     doi:10.1128/AEM.01176-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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