Lipid-protein interactions in membranes: effect of lipid composition on mobility of spin-labeled cysteine residues in yeast plasma membrane.
In order to gain direct evidence for lipid-dependent protein conformation in membrane, effects of modification of lipid composition on mobility of spin-labeled cysteine residues were investigated in the plasma membrane of the yeast Saccharomyces cerevisiae. Conversion of the bulk of phospholipids to diglycerides by treatment of the membrane with phospholipase C substantially enhanced spectral anisotropy. However, alterations of the viscosity of the lipid-bilayer by enriching the membrane with palmitelaidic or oleic acid had no effect on mobility of spin-labeled cysteine residues. These observations indicate that while the spin-labeled residues are not in direct contact with the lipid core of the membrane, there are lipid-protein interactions to the extent that removal of the polar portion of the bulk of phospholipids induces conformational changes in proteins, which in turn restrict mobility of these residues. It is concluded that conformation of membrane proteins on lipid structure and that phospholipids have a role in preserving the native conformation of proteins.
D000251:Adenosine Triphosphatases / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003545:Cysteine; D004075:Diglycerides; D004578:Electron Spin Resonance Spectroscopy; D005227:Fatty Acids / Q000032:analysis; D008563:Membrane Lipids / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D010743:Phospholipids / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000648:ultrastructure*; D013113:Spin Labels; D010738:Type C Phospholipases
D004075:Diglycerides; D005227:Fatty Acids; D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D013113:Spin Labels; D010738:Type C Phospholipases; D000251:Adenosine Triphosphatases; D003545:Cysteine