Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 18-22 |
| Seitenumfang | 5 |
| Fachzeitschrift | FEBS Letters |
| Jahrgang | 550 |
| Ausgabenummer | 1-3 |
| Publikationsstatus | Veröffentlicht - 28 Aug. 2003 |
Abstract
Translocation of folded proteins across biological membranes can be mediated by the so-called 'twin-arginine translocation' (Tat) system. To be translocated, Tat substrates require N-terminal signal sequences which usually contain the eponymous twin-arginine motif. Here we report the first structural analysis of a twin-arginine signal sequence, the signal sequence of the high potential iron-sulfur protein from Allochromatium vinosum. Nuclear magnetic resonance (NMR) analyses of amide proton resonances did not indicate a signal sequence structure. Accordingly, data from H/D exchange matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry showed that the amide protons of the signal sequence exchange rapidly, indicating the absence of secondary structure in the signal sequence up to L29. We conclude that the conserved twin-arginine motif does not form a structure by itself or as a result of intramolecular interactions.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biophysik
- Biochemie, Genetik und Molekularbiologie (insg.)
- Strukturelle Biologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: FEBS Letters, Jahrgang 550, Nr. 1-3, 28.08.2003, S. 18-22.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Structural studies on a twin-arginine signal sequence
AU - Kipping, Marc
AU - Lilie, Hauke
AU - Lindenstrauß, Ute
AU - Andreesen, Jan R.
AU - Griesinger, Christian
AU - Carlomagno, Teresa
AU - Brüser, Thomas
N1 - Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft with grant BR2285/1-1 to T.B. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2003/8/28
Y1 - 2003/8/28
N2 - Translocation of folded proteins across biological membranes can be mediated by the so-called 'twin-arginine translocation' (Tat) system. To be translocated, Tat substrates require N-terminal signal sequences which usually contain the eponymous twin-arginine motif. Here we report the first structural analysis of a twin-arginine signal sequence, the signal sequence of the high potential iron-sulfur protein from Allochromatium vinosum. Nuclear magnetic resonance (NMR) analyses of amide proton resonances did not indicate a signal sequence structure. Accordingly, data from H/D exchange matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry showed that the amide protons of the signal sequence exchange rapidly, indicating the absence of secondary structure in the signal sequence up to L29. We conclude that the conserved twin-arginine motif does not form a structure by itself or as a result of intramolecular interactions.
AB - Translocation of folded proteins across biological membranes can be mediated by the so-called 'twin-arginine translocation' (Tat) system. To be translocated, Tat substrates require N-terminal signal sequences which usually contain the eponymous twin-arginine motif. Here we report the first structural analysis of a twin-arginine signal sequence, the signal sequence of the high potential iron-sulfur protein from Allochromatium vinosum. Nuclear magnetic resonance (NMR) analyses of amide proton resonances did not indicate a signal sequence structure. Accordingly, data from H/D exchange matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry showed that the amide protons of the signal sequence exchange rapidly, indicating the absence of secondary structure in the signal sequence up to L29. We conclude that the conserved twin-arginine motif does not form a structure by itself or as a result of intramolecular interactions.
KW - H/D exchange matrix-assisted laser desorption/ionization-time of flight mass spectrometry
KW - High potential iron-sulfur protein
KW - Nuclear magnetic resonance
KW - Protein translocation
KW - Signal sequence
KW - Twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=0142102531&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(03)00804-4
DO - 10.1016/S0014-5793(03)00804-4
M3 - Article
C2 - 12935879
AN - SCOPUS:0142102531
VL - 550
SP - 18
EP - 22
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-3
ER -