Journal
FEBS JOURNAL
Volume 275, Issue 24, Pages 6159-6167Publisher
WILEY
DOI: 10.1111/j.1742-4658.2008.06740.x
Keywords
halophilic archaea; protein translocation; signal peptide; sodium motive force; twin-arginine translocase
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Funding
- Biotechnology and Biological Sciences Research Council
- Royal Society University
- Biotechnology and Biological Sciences Research Council [C19762] Funding Source: researchfish
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Twin-arginine translocase (Tat) is involved in the translocation of fully folded proteins in a process that is driven by the proton motive force. In most prokaryotes, the Tat system transports only a small proportion of secretory proteins, and Tat substrates are often cofactor-containing proteins that require folding before translocation. A notable exception is found in halophilic archaea (haloarchaea), which are predicted to secrete the majority of their proteins through the Tat pathway. In this study, we have analysed the translocation of a secretory protein (AmyH) from the haloarchaeon Haloarcula hispanica. Using both in vivo and in vitro translocation assays, we demonstrate that AmyH transport is Tat-dependent, and, surprisingly, that its secretion does not depend on the proton motive force but requires the sodium motive force instead.
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