Functional Reconstitution of Membrane Proteins in Monolayer Liposomes from Bipolar Lipids of Sulfolobus acidocaldariusElferink, M., Wit, J. G. D., Demel, R., Driessen, A. J. M. & Konings, W., 15-Jan-1992, In : The Journal of Biological Chemistry. 267, 2, p. 1375-1381 7 p.
Research output: Contribution to journal › Article › Academic › peer-review
Membranes of Sulfolobus acidocaldarius, an extreme thermophilic archaebacterium, are composed of unusual bipolar lipids. They consist of macrocyclic tetraethers with two polar heads linked by two hydrophobic C40 phytanyl chains which are thought to be arranged as a monolayer in the cytoplasmic membrane. Fractionation of a total lipid-extract from S. acidocaldarius yielded a lipid fraction which forms closed and stable unilamellar liposomes in aqueous media. Beef heart cytochrome c-oxidase could be functionally reconstituted in these liposomes. In the presence of reduced cytochrome c, a protonmotive force (Δp) across the liposomal membrane was generated of up to -92 mV. Upon fusion of these proteoliposomes with membrane vesicles of Lactococcus lactis, the Δp generated by cytochrome c-oxidase activity was capable to drive uphill transport of leucine. Electron microscopic analysis indicated that the tetraether lipids form a single monolayer liposome. The results demonstrate that tetraether lipids of archaebacteria can form a suitable matrix for the function of exogenous membrane proteins originating from a regular lipid bilayer.
|Number of pages||7|
|Journal||The Journal of Biological Chemistry|
|Publication status||Published - 15-Jan-1992|
- PROTON-MOTIVE FORCE, THERMOPHILIC ARCHAEBACTERIA, STREPTOCOCCUS-CREMORIS, BLACK MEMBRANES, ETHER LIPIDS, CYTOCHROME-C, VESICLES, OXIDASE, PURIFICATION, TEMPERATURE