JBC, Vol. 252, Issue 10, 3208-3213, May, 1977
Selective incorporation of membrane proteins into proteoliposomes of different compositions
G. D. Eytan and E. Racker
1. Cytochrome oxidase was incorporated into preformed liposomes containing
phosphatidylserine. When confronted with a mixture of liposomes, some
containing phosphatidylserine and some without it, the enzyme was
incorporated only into the phosphatidylserine-containing liposomes. 2. The
hydrophobic proteins of the oligomycin-sensitive ATPase incubated in the
presence of a mixture of liposomes with and without cytochrome oxidase were
preferentially incorporated into cytochrome oxidase-containing liposomes.
This selectivity was abolished by either cytochrome c or ascorbate. 3.
Cytochrome oxidase incubated in the presence of a mixture of liposomes with
and without the hydrophobic proteins of the ATPase was preferentially
incorporated into liposomes that did not contain the hydrophobic proteins.
4. Cytochrome oxidase and the oligomycin-sensitive ATPase were
preferentially incorporated into pure liposomes over
bacteriorhodopsin-containing vesicles. 5. Reduced coenzyme Q
(QH2)-cytochrome c reductase was incorporated randomly when incubated in
the presence of a mixture of pure liposomes and liposomes containing the
hydrophobic proteins of the ATPase complex. 6. The significance of the
incorporation procedure as a model for membrane biogenesis is discussed.
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