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)