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• W1514781231 startingPage "6159" @default.
• W1514781231 abstract "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." @default.
• W1514781231 created "2016-06-24" @default.
• W1514781231 creator A5008967284 @default.
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• W1514781231 date "2008-11-05" @default.
• W1514781231 modified "2023-09-27" @default.
• W1514781231 title "Bioenergetic requirements of a Tat-dependent substrate in the halophilic archaeon Haloarcula hispanica" @default.
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• W1514781231 doi "https://doi.org/10.1111/j.1742-4658.2008.06740.x" @default.
• W1514781231 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19016855" @default.
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