Structural studies on a twin-arginine signal sequence

verfasst von

Marc Kipping, Hauke Lilie, Ute Lindenstrauß, Jan R. Andreesen, Christian Griesinger, Teresa Carlomagno, Thomas Brüser

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.

Organisationseinheit(en)

Institut für Mikrobiologie

Externe Organisation(en)

Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung
Martin-Luther-Universität Halle-Wittenberg
Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut)

Typ

Artikel

Journal

FEBS Letters

Band

550

Seiten

18-22

Anzahl der Seiten

5

ISSN

0014-5793

Publikationsdatum

28.08.2003

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Biophysik, Strukturelle Biologie, Biochemie, Molekularbiologie, Genetik, Zellbiologie

Elektronische Version(en)

https://doi.org/10.1016/S0014-5793(03)00804-4 (Zugang: Unbekannt)