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J. Biol. Chem., Vol. 269, Issue 4, 2508-2515, 01, 1994
E Winkler and M Klingenberg
A detailed study on the activation of H+ transport by reconstituted
uncoupling proteins from brown adipose tissue is given, including the
influence of chain lengths and of other structural modifications,
concentration dependence, and the influence of nucleotides. Uncoupling
protein was reconstituted with phosphatidylcholine in such a way as to keep
H+ transport with endogenous fatty acids at a minimum. Using excess of
polystyrene beads on reconstitution avoided the complications arising from
the use of albumin. Both delta psi-driven H+ uptake and H+ efflux systems
are used by changing the polarity. Fatty acids stimulate H+ uptake up to
6-fold and H+ efflux more than 10-fold. There is no competition between the
inhibition by nucleotides (GTP) and fatty acids. Also, the binding of GTP
and ATP is not affected. Only fatty acids starting from C8 activate,
reaching a maximum at C14. However, unsaturated homologous of C18 (oleic,
linoleic, etc.) are fully active. Hydrophilic substitutions by hydroxyl,
CO2H, bromo, doxyl groups also permit good activation, probably due to
improved uptake into the lipid phase. The hydrophobic moiety exhibits a low
specificity. Blockage of carboxyl by esterification abolishes the
activation. Maximum activation requires high total concentrations of
200-300 microM. The distribution of fatty acids between proteoliposomes and
solution was determined. The activation mode of fatty acids is discussed
either as regulatory activators or as cofactors in H+ translocation
involving their carboxyl groups. Two alternatives are considered, namely
that the fatty acids carboxyl group is at the translocation center or in
the channel facilitating H+ transfer to the constituent H(+)-translocating
carboxyl groups.
Effect of fatty acids on H+ transport activity of the reconstituted uncoupling protein
Institute for Physical Biochemistry, University of Munich, Federal Republic of Germany.
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