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Review Article

Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins

Nicola J. Harris, Kalypso Charalambous, Heather E. Findlay, Paula J. Booth
Biochemical Society Transactions Sep 06, 2018, 46 (5) 1355-1366; DOI: 10.1042/BST20170424
Nicola J. Harris
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
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Kalypso Charalambous
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
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Heather E. Findlay
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
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Paula J. Booth
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
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  • For correspondence: paula.booth@kcl.ac.uk
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Abstract

Membrane proteins must be inserted into a membrane and folded into their correct structure to function correctly. This insertion occurs during translation and synthesis by the ribosome for most α-helical membrane proteins. Precisely how this co-translational insertion and folding occurs, and the role played by the surrounding lipids, is still not understood. Most of the work on the influence of the lipid environment on folding and insertion has focussed on denatured, fully translated proteins, and thus does not replicate folding during unidirectional elongation of nascent chains that occurs in the cell. This review aims to highlight recent advances in elucidating lipid composition and bilayer properties optimal for insertion and folding of nascent chains in the membrane and in the assembly of oligomeric proteins.

  • lipid bilayer
  • lipid composition
  • protein folding
  • transmembrane proteins
  • Abbreviations

    DEPG,
    1,2-dielaidoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (18:1 (Δ9-trans) PS);
    DMPC,
    1,2-dimyristoyl-sn-glycero-3-phosphocholine (14:0 PC);
    DMPG,
    1,2-dimyristoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (14:0 PG);
    DOPC,
    1,2-dioleoyl-sn-glycero-3-phosphocholine (18:1 (Δ9-cis) PC);
    DOPE,
    1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (18:1 (Δ9-cis) PE);
    DOPG,
    1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (18:1 (Δ9-cis) PG);
    DOPS,
    1,2-dioleoyl-sn-glycero-3-phospho-L-serine (18:1 (Δ9-cis) PS);
    DPPC,
    1,2-dipalmitoyl-sn-glycero-3-phosphocholine (16:0 PC);
    PC,
    phosphocholine;
    PE,
    phosphoethanolamine;
    PG,
    phosphoglycerol;
    PI,
    phosphoinositol;
    PS,
    phosphoserine;
    SRP,
    signal recognition particle;
    TM,
    transmembrane
    • © 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
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    October 2018

    Volume: 46 Issue: 5

    Biochemical Society Transactions: 46 (5)
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    Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins
    Nicola J. Harris, Kalypso Charalambous, Heather E. Findlay, Paula J. Booth
    Biochemical Society Transactions Oct 2018, 46 (5) 1355-1366; DOI: 10.1042/BST20170424
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    Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins
    Nicola J. Harris, Kalypso Charalambous, Heather E. Findlay, Paula J. Booth
    Biochemical Society Transactions Oct 2018, 46 (5) 1355-1366; DOI: 10.1042/BST20170424

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    • Article
      • Abstract
      • Introduction
      • Why study nascent chain folding?
      • Nascent chain folding in vivo
      • Lipids modulate folding and insertion of membrane proteins
      • Lipids and cell-free expression of membrane proteins
      • Optimising the surrounding lipids promotes nascent chain folding
      • Making oligomeric membrane proteins using cell-free expression
      • Cell-free expression of the homopentameric channel MscL
      • Conclusions
      • Funding
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      • References
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    Keywords

    lipid bilayer
    lipid composition
    protein folding
    transmembrane proteins

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