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Applied and Environmental Microbiology, December 2008, p. 7507-7513, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.01401-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

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{triangledown}

Marc A. B. Kolkman,1,# René van der Ploeg,2,# Michael Bertels,1 Maurits van Dijk,2 Joop van der Laan,3 Jan Maarten van Dijl,2* and Eugenio Ferrari3

Genencor, a Danisco Division, Archimedesweg 30, 2333 CN Leiden, The Netherlands,1 Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Hanzeplein 1, P.O. Box 30001, 9700 RB Groningen, The Netherlands,2 Genencor, a Danisco Division, 925 Page Mill Road, Palo Alto, California 943043

Received 23 June 2008/ Accepted 13 October 2008

Proteins that are produced for commercial purposes in Bacillus subtilis are commonly secreted via the Sec pathway. Despite its high secretion capacity, the secretion of heterologous proteins via the Sec pathway is often unsuccessful. Alternative secretion routes, like the Tat pathway, are therefore of interest. Two parallel Tat pathways with distinct specificities have previously been discovered in B. subtilis. To explore the application potential of these Tat pathways, several commercially relevant or heterologous model proteins were fused to the signal peptides of the known B. subtilis Tat substrates YwbN and PhoD. Remarkably, the YwbN signal peptide directed secretion of active subtilisin, a typical Sec substrate, via the B. subtilis TatAyCy route. In contrast, the same signal peptide directed Tat-independent secretion of the Bacillus licheniformis {alpha}-amylase (AmyL). Moreover, the YwbN signal peptide directed secretion of SufI, an Escherichia coli Tat substrate, in a Tat-independent manner, most likely via Sec. Our results suggest that cytoplasmic protein folding prior to translocation is probably a major determinant of Tat-dependent protein secretion in B. subtilis, as is the case with E. coli. We conclude that future applications for the Tat system of B. subtilis will most likely involve commercially interesting proteins that are Sec incompatible.

* 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 3615187. Fax: 31 50 3619105. E-mail: j.m.van.dijl{at}med.umcg.nl

{triangledown} Published ahead of print on 17 October 2008.

# These authors contributed equally to this work.

Applied and Environmental Microbiology, December 2008, p. 7507-7513, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.01401-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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