Structural studies on a twin-arginine signal sequence

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Authors

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

Research Organisations

External Research Organisations

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

Original languageEnglish
Pages (from-to)18-22
Number of pages5
JournalFEBS Letters
Volume550
Issue number1-3
Publication statusPublished - 28 Aug 2003

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.

Keywords

    H/D exchange matrix-assisted laser desorption/ionization-time of flight mass spectrometry, High potential iron-sulfur protein, Nuclear magnetic resonance, Protein translocation, Signal sequence, Twin-arginine translocation

ASJC Scopus subject areas

Cite this

Structural studies on a twin-arginine signal sequence. / Kipping, Marc; Lilie, Hauke; Lindenstrauß, Ute et al.
In: FEBS Letters, Vol. 550, No. 1-3, 28.08.2003, p. 18-22.

Research output: Contribution to journal › Article › Research › peer review

Kipping, M, Lilie, H, Lindenstrauß, U, Andreesen, JR, Griesinger, C, Carlomagno, T & Brüser, T 2003, 'Structural studies on a twin-arginine signal sequence', FEBS Letters, vol. 550, no. 1-3, pp. 18-22. https://doi.org/10.1016/S0014-5793(03)00804-4
Kipping, M., Lilie, H., Lindenstrauß, U., Andreesen, J. R., Griesinger, C., Carlomagno, T., & Brüser, T. (2003). Structural studies on a twin-arginine signal sequence. FEBS Letters, 550(1-3), 18-22. https://doi.org/10.1016/S0014-5793(03)00804-4
Kipping M, Lilie H, Lindenstrauß U, Andreesen JR, Griesinger C, Carlomagno T et al. Structural studies on a twin-arginine signal sequence. FEBS Letters. 2003 Aug 28;550(1-3):18-22. doi: 10.1016/S0014-5793(03)00804-4
Kipping, Marc ; Lilie, Hauke ; Lindenstrauß, Ute et al. / Structural studies on a twin-arginine signal sequence. In: FEBS Letters. 2003 ; Vol. 550, No. 1-3. pp. 18-22.
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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.",
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AU - Kipping, Marc

AU - Lilie, Hauke

AU - Lindenstrauß, Ute

AU - Andreesen, Jan R.

AU - Griesinger, Christian

AU - Carlomagno, Teresa

AU - Brüser, Thomas

N1 - Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft with grant BR2285/1-1 to T.B. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

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N2 - 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.

AB - 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.

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