Phosphatidylglycerol lipids enhance folding of an alpha helical membrane protein.
Membrane lipids are increasingly being recognised as active participants in biological events. The precise roles that individual lipids or global properties of the lipid bilayer play in the folding of membrane proteins remain to be elucidated, Here, we find a significant effect of phosphatidylglycerol (PG) on the folding of a trimeric alpha helical membrane protein from Escherichia coli diacylglycerol kinase. Both the rate and the yield of folding are increased by increasing the amount of PG in lipid vesicles. Moreover, there is a direct correlation between the increase in yield and the increase in rate; thus, folding becomes more efficient in terms of speed and productivity. This effect of PG seems to be a specific requirement for this lipid, rather than a charge effect. We also find an effect of single-chain lyso lipids in decreasing the rate and yield of folding. We compare this to our previous work in which lyso lipids increased the rate and yield of another membrane protein, bacteriorhodopsin. The contrasting effect of lyso lipids on the two proteins can be explained by the different folding reaction mechanisms and key folding steps involved. Our findings provide information on the lipid determinants of membrane protein folding.
Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK. a.seddon@imperial.ac.uk
Annela M
AM
Seddon
Mark
M
Lorch
Oscar
O
Ces
Richard H
RH
Templer
Fiona
F
Macrae
Paula J
PJ
Booth
D019852:Diacylglycerol Kinase / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D010715:Phosphatidylglycerols / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D010715:Phosphatidylglycerols; D019852:Diacylglycerol Kinase