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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/33423
Title: The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis
Authors: Sariqa Wagley
Claudia Hemsley
Rachael Thomas
Madeleine G. Moule
Muthita Vanaporn
Clio Andreae
Matthew Robinson
Stan Goldman
Brendan W. Wren
Clive S. Butler
Richard W. Titball
University of Exeter
London School of Hygiene & Tropical Medicine
Mahidol University
Evolva Inc.
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-Jan-2014
Citation: Journal of Bacteriology. Vol.196, No.2 (2014), 407-416
Abstract: The twin arginine translocation (Tat) system in bacteria is responsible for transporting folded proteins across the cytoplasmic membrane, and in some bacteria, Tat-exported substrates have been linked to virulence. We report here that the Tat machinery is present in Burkholderia pseudomallei, B. mallei, and B. thailandensis, and we show that the system is essential for aerobic but not anaerobic growth. Switching off of the Tat system in B. thailandensis grown anaerobically resulted in filamentous bacteria, and bacteria showed increased sensitivity to some ß-lactam antibiotics. In Galleria mellonella and zebrafish infection models, the Tat conditional mutant was attenuated. The aerobic growth-restricted phenotype indicates that Tat substrates may play a functional role in oxygen-dependent energy conservation. In other bacteria, aerobic growth restriction in Tat mutants has been attributed to the inability to translocate PetA, the Rieske iron-sulfur protein which forms part of the quinol-cytochrome c oxidoreductase complex. Here, we show that PetA is not responsible for aerobic growth restriction in B. thailandensis. However, we have identified an operon encoding 2 proteins of unknown function (BTH_I2176 and BTH_I2175) that play a role in aerobic growth restriction, and we present evidence that BTH_I2176 is Tat translocated. © 2014, American Society for Microbiology. All Rights Reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84890940586&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/33423
ISSN: 10985530
00219193
Appears in Collections:Scopus 2011-2015

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