van der Ploeg, René, Mäder, Ulrike, Homuth, Georg, Schaffer, Marc, Denham, Emma, Monteferrante, Carmine G., Miethke, Marcus, Marahiel, Mohamed A., Harwood, Colin R., Winter, Theresa, Hecker, Michael, Antelmann, Haike and Dijl, Jan Maarten van (2011) Environmental salinity determines the specificity and need for tat-dependent secretion of the YwbN protein in bacillus subtilis. PLoS One, Volume 6 (Number 3). Article number e18140. doi:10.1371/journal.pone.0018140 ISSN 1932-6203.

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Abstract

Twin-arginine protein translocation (Tat) pathways are required for transport of folded proteins across bacterial, archaeal and chloroplast membranes. Recent studies indicate that Tat has evolved into a mainstream pathway for protein secretion in certain halophilic archaea, which thrive in highly saline environments. Here, we investigated the effects of environmental salinity on Tat-dependent protein secretion by the Gram-positive soil bacterium Bacillus subtilis, which encounters widely differing salt concentrations in its natural habitats. The results show that environmental salinity determines the specificity and need for Tat-dependent secretion of the Dyp-type peroxidase YwbN in B. subtilis. Under high salinity growth conditions, at least three Tat translocase subunits, namely TatAd, TatAy and TatCy, are involved in the secretion of YwbN. Yet, a significant level of Tat-independent YwbN secretion is also observed under these conditions. When B. subtilis is grown in medium with 1% NaCl or without NaCl, the secretion of YwbN depends strictly on the previously described “minimal Tat translocase” consisting of the TatAy and TatCy subunits. Notably, in medium without NaCl, both tatAyCy and ywbN mutants display significantly reduced exponential growth rates and severe cell lysis. This is due to a critical role of secreted YwbN in the acquisition of iron under these conditions. Taken together, our findings show that environmental conditions, such as salinity, can determine the specificity and need for the secretion of a bacterial Tat substrate.

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH301 Biology Q Science > QR Microbiology
Divisions:	Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Microbiology & Infection Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH):	Bacillus subtilis, Salinity, Proteins -- Research, Bacillus (Bacteria)
Journal or Publication Title:	PLoS One
Publisher:	Public Library of Science
ISSN:	1932-6203
Official Date:	2011
Dates:	Date Event 2011 Published
Volume:	Volume 6
Number:	Number 3
Page Range:	Article number e18140
DOI:	10.1371/journal.pone.0018140
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Open Access (Creative Commons)
Date of first compliant deposit:	26 December 2015
Date of first compliant Open Access:	26 December 2015
Funder:	European Commission (EC), Systems Biology of Microorganisms (SysMO), European Science Foundation (ESF), Nederlandse Organisatie voor Wetenschappelijk Onderzoek [Netherlands Organisation for Scientific Research] (NWO), Deutsche Forschungsgemeinschaft (DFG), Fonds der Chemischen Industrie (Germany) (FCI), Germany. Bundesministerium für Bildung und Forschung (BMBF)
Grant number:	LSHG-CT-2004-503468, LSHG-CT-2004-005257, LSHM-CT-2006-019064, LSHG-CT-2006-037469, PITN-GA-2008-215524 (EC) ; 04-EScope 01-011 (NWO) ; 03ZIK012 (BMBF)

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