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J. Biol. Chem., Vol. 282, Issue 46, 33257-33264, November 16, 2007

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Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins^*

Silke Richter, Ute Lindenstrauss, Christian Lücke, Richard Bayliss^¶1, and Thomas Brüser²

From the Institute of Biology/Microbiology, University of Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle, Germany, the Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle, Germany, and the ^¶Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom

The twin-arginine translocation (Tat) system is a protein translocation system that is adapted to the translocation of folded proteins across biological membranes. An understanding of the folding requirements for Tat substrates is of fundamental importance for the elucidation of the transport mechanism. We now demonstrate for the first time Tat transport for fully unstructured proteins, using signal sequence fusions to naturally unfolded FG repeats from the yeast Nsp1p nuclear pore protein. The transport of unfolded proteins becomes less efficient with increasing size, consistent with only a single interaction between the system and the substrate. Strikingly, the introduction of six residues from the hydrophobic core of a globular protein completely blocked translocation. Physiological data suggest that hydrophobic surface patches abort transport at a late stage, most likely by membrane interactions during transport. This study thus explains the observed restriction of the Tat system to folded globular proteins on a molecular level.

Received for publication, April 19, 2007 , and in revised form, September 10, 2007.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant BR2285/1-3 and grants from the state Sachsen-Anhalt (Exzellenz-Cluster Biowissenschaften) and the Fonds der Chemischen Industrie (to T. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ Supported by the Royal Society and the Institute of Cancer Research.

² To whom correspondence should be addressed. Tel.: 49-345-5526360; E-mail: t.brueser{at}mikrobiologie.uni-halle.de.

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