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Recognition of transmembrane helices by the endoplasmic reticulum translocon

Author

Listed:
  • Tara Hessa

    (Stockholm University)

  • Hyun Kim

    (Stockholm University)

  • Karl Bihlmaier

    (Stockholm University
    Institute of Biochemistry, ETH Zurich)

  • Carolina Lundin

    (Stockholm University)

  • Jorrit Boekel

    (Stockholm University)

  • Helena Andersson

    (Karolinska Institutet, Department of Bioscience at NOVUM)

  • IngMarie Nilsson

    (Stockholm University)

  • Stephen H. White

    (University of California at Irvine)

  • Gunnar von Heijne

    (Stockholm University)

Abstract

Membrane proteins depend on complex translocation machineries for insertion into target membranes. Although it has long been known that an abundance of nonpolar residues in transmembrane helices is the principal criterion for membrane insertion, the specific sequence-coding for transmembrane helices has not been identified. By challenging the endoplasmic reticulum Sec61 translocon with an extensive set of designed polypeptide segments, we have determined the basic features of this code, including a ‘biological’ hydrophobicity scale. We find that membrane insertion depends strongly on the position of polar residues within transmembrane segments, adding a new dimension to the problem of predicting transmembrane helices from amino acid sequences. Our results indicate that direct protein–lipid interactions are critical during translocon-mediated membrane insertion.

Suggested Citation

  • Tara Hessa & Hyun Kim & Karl Bihlmaier & Carolina Lundin & Jorrit Boekel & Helena Andersson & IngMarie Nilsson & Stephen H. White & Gunnar von Heijne, 2005. "Recognition of transmembrane helices by the endoplasmic reticulum translocon," Nature, Nature, vol. 433(7024), pages 377-381, January.
    • Handle: RePEc:nat:nature:v:433:y:2005:i:7024:d:10.1038_nature03216
    DOI: 10.1038/nature03216
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    Cited by:

    1. Mika Ito & Jan Johansson & Roger Strömberg & Lennart Nilsson, 2011. "Unfolding of the Amyloid β-Peptide Central Helix: Mechanistic Insights from Molecular Dynamics Simulations," PLOS ONE, Public Library of Science, vol. 6(3), pages 1-13, March.

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