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Title: Functional Tat transport of unstructured, small, hydrophilic proteins.
Authors: Richter, S
Lindenstrauss, U
Lücke, C
Bayliss, R
Brüser, T
First Published: 16-Nov-2007
Citation: J BIOL CHEM, 2007, 282 (46), pp. 33257-33264
Abstract: 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.
DOI Link: 10.1074/jbc.M703303200
ISSN: 0021-9258
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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