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- Title
Structural studies on a twin-arginine signal sequence
- Authors
Kipping, Marc; Lilie, Hauke; Lindenstrauß, Ute; Andreesen, Jan R.; Griesinger, Christian; Carlomagno, Teresa; Brüser, Thomas
- 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.
- Subjects
CHROMOSOMAL translocation; MEMBRANE proteins; NUCLEAR magnetic resonance; ARGININE
- Publication
FEBS Letters, 2003, Vol 550, Issue 1-3, p18
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)00804-4