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Structural studies on a twin‐arginine signal sequence
Author(s) -
Kipping Marc,
Lilie Hauke,
Lindenstrauß Ute,
Andreesen Jan R,
Griesinger Christian,
Carlomagno Teresa,
Brüser Thomas
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00804-4
Subject(s) - arginine , chemistry , signal peptide , mass spectrometry , peptide sequence , amide , biophysics , crystallography , biochemistry , nuclear magnetic resonance , amino acid , biology , physics , chromatography , gene
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.