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

doi:10.1042/BST20170424

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

Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K. [email protected].

Research output: Contribution to journal › Review article › peer-review

22 Citations (Scopus)

326 Downloads (Pure)

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.

Original language	English
Journal	Biochemical Society Transactions
Early online date	6 Sept 2018
DOIs	https://doi.org/10.1042/BST20170424
Publication status	E-pub ahead of print - 6 Sept 2018

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Lipids modulate the insertion_HARRIS_Firstonline6September2018_GREEN AAM Accepted author manuscript, 1.26 MB

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title = "Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins",

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.",

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AU - Harris, Nicola J

AU - Charalambous, Kalypso

AU - Findlay, Heather E

AU - Booth, Paula J

PY - 2018/9/6

Y1 - 2018/9/6

N2 - 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.

AB - 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.

U2 - 10.1042/BST20170424

DO - 10.1042/BST20170424

M3 - Review article

C2 - 30190329

SN - 0300-5127

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -

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

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