Lipid-protein interactions in stacked and destacked thylakoid membranes and the influence of phosphorylation and illumination. Spin label ESR studies.
The effects of membrane destacking, protein phosphorylation, and continuous illumination have been studied in pea thylakoid membranes using ESR spectroscopy of an incorporated spin-labelled phosphatidylglycerol. This spin-labelled analogue of an endogenous thylakoid lipid has previously been shown to exhibit a selectivity of interaction with thylakoid proteins. Neither destacking, phosphorylation nor illumination was found to change the ESR spectra appreciably, suggesting that for phosphatidylglycerol at least, neither the number of protein-associated membrane lipids nor their pattern of selectivity was altered. The redistribution of the thylakoid protein complexes in the membrane, under these various conditions, therefore takes place with conservation of the properties of the lipid/protein interface.
Li
G
G
Astbury Department of Biophysics, University of Leeds, U.K.
Knowles
P F
PF
Murphy
D J
DJ
Marsh
D
D
D002462:Cell Membrane / Q000648:ultrastructure; D002736:Chloroplasts / Q000648:ultrastructure*; D004578:Electron Spin Resonance Spectroscopy; D007887:Fabaceae; D008027:Light; D008565:Membrane Proteins / Q000032:analysis*; D010715:Phosphatidylglycerols; D010766:Phosphorylation; D010940:Plant Proteins; D010946:Plants, Medicinal; D011487:Protein Conformation; D013113:Spin Labels
D008565:Membrane Proteins; D010715:Phosphatidylglycerols; D010940:Plant Proteins; D013113:Spin Labels; C042085:thylakoid membrane phosphoprotein, plant