The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis
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. mal...
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th-mahidol.334232018-11-09T09:25:17Z The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis 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. Biochemistry, Genetics and Molecular Biology Immunology and Microbiology 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. 2018-11-09T01:58:20Z 2018-11-09T01:58:20Z 2014-01-01 Article Journal of Bacteriology. Vol.196, No.2 (2014), 407-416 10.1128/JB.01046-13 10985530 00219193 2-s2.0-84890940586 https://repository.li.mahidol.ac.th/handle/123456789/33423 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84890940586&origin=inward |
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Biochemistry, Genetics and Molecular Biology Immunology and Microbiology 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 The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
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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. |
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University of Exeter |
author_facet |
University of Exeter 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 |
format |
Article |
author |
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 |
author_sort |
Sariqa Wagley |
title |
The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
title_short |
The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
title_full |
The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
title_fullStr |
The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
title_full_unstemmed |
The twin arginine translocation system is essential for aerobic growth and full virulence of Burkholderia thailandensis |
title_sort |
twin arginine translocation system is essential for aerobic growth and full virulence of burkholderia thailandensis |
publishDate |
2018 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/33423 |
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1763497276972466176 |