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Related Experiment Videos

Transmembrane helices before, during, and after insertion.

Stephen H White1, Gunnar von Heijne

  • 1Department of Physiology and Biophysics, and Program in Macromolecular Structure, University of California at Irvine, Irvine, CA 92697-4560, USA. blanco@helium.biomol.uci.edu

Current Opinion in Structural Biology
|July 27, 2005
PubMed
Summary

Researchers have deciphered the code governing how transmembrane (TM) helices insert into proteins. This breakthrough explains how helix-bundle membrane proteins are built, advancing our understanding of cellular machinery.

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Area of Science:

  • Structural biology
  • Membrane protein biophysics
  • Molecular machinery

Background:

  • Transmembrane (TM) helices are essential building blocks for helix-bundle membrane proteins.
  • Understanding TM helix interactions and insertion is crucial for deciphering protein biogenesis.
  • The translocon complex, working with ribosomes, facilitates biological helix insertion.

Purpose of the Study:

  • To elucidate the fundamental code dictating TM helix selection and insertion by the translocon.
  • To provide new insights into the architecture and function of the translocon complex.
  • To analyze the structural basis of TM helix interactions within membrane protein bundles.

Main Methods:

  • Electron cryo-microscopic reconstruction of translocon complexes.

Related Experiment Videos

  • Disulfide bridge studies to track polypeptide chain passage.
  • Analysis of amino acid distributions in known helix-bundle membrane proteins.

    • Main Results:

    • Detailed architecture of the translocon complex, comprising SecY/Sec61 heterotrimers and TRAP complexes.
    • Confirmation of polypeptide chain transit through the SecY pore during insertion.
    • Deciphering the code that governs the selection of TM helix segments.

    Conclusions:

    • The fundamental code for TM helix insertion by the translocon has been identified.
    • Structural analysis of membrane proteins recapitulates this code.
    • This work advances the understanding of membrane protein biogenesis and function.