Kwan, Daniel C., Thomas, Judith R. and Bolhuis, Albert. (2008) Bioenergetic requirements of a Tat-dependent substrate in the halophilic archaeon Haloarcula hispanica. The FEBS Journal, Vol.275 (No.24). pp. 6159-6167. ISSN 1742-464X

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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.

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Item Type:	Journal Article
Subjects:	Q Science > QP Physiology Q Science > QR Microbiology
Divisions:	Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH):	Halophilic microorganisms, Proteins -- Physiological transport, Cellular signal transduction, Bioenergetics
Journal or Publication Title:	The FEBS Journal
Publisher:	Wiley-Blackwell Publishing Ltd.
ISSN:	1742-464X
Date:	December 2008
Volume:	Vol.275
Number:	No.24
Number of Pages:	9
Page Range:	pp. 6159-6167
Identification Number:	10.1111/j.1742-4658.2008.06740.x
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Royal Society (Great Britain), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC)
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URI:	http://wrap.warwick.ac.uk/id/eprint/28978

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