Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 33257-33264 |
| Seitenumfang | 8 |
| Fachzeitschrift | Journal of Biological Chemistry |
| Jahrgang | 282 |
| Ausgabenummer | 46 |
| Publikationsstatus | Veröffentlicht - 16 Nov. 2007 |
| Extern publiziert | Ja |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Journal of Biological Chemistry, Jahrgang 282, Nr. 46, 16.11.2007, S. 33257-33264.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Functional tat transport of unstructured, small, hydrophilic proteins
AU - Richter, Silke
AU - Lindenstrauss, Ute
AU - Lücke, Christian
AU - Bayliss, Richard
AU - Brüser, Thomas
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2007/11/16
Y1 - 2007/11/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=36348950408&partnerID=8YFLogxK
U2 - 10.1074/jbc.M703303200
DO - 10.1074/jbc.M703303200
M3 - Article
C2 - 17848553
AN - SCOPUS:36348950408
VL - 282
SP - 33257
EP - 33264
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 46
ER -