Structural studies on a twin-arginine signal sequence

authored by

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.

Organisation(s)

Institute of Microbiology

External Organisation(s)

Max Planck Research Unit for Enzymology of Protein Folding
Martin Luther University Halle-Wittenberg
Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute)

Type

Article

Journal

FEBS Letters

Volume

550

Pages

18-22

No. of pages

5

ISSN

0014-5793

Publication date

28.08.2003

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Biophysics, Structural Biology, Biochemistry, Molecular Biology, Genetics, Cell Biology

Electronic version(s)

https://doi.org/10.1016/S0014-5793(03)00804-4 (Access: Unknown)