Cysteine residues are not essential for uncoupling protein function

Author:

Arechaga I1,Raimbault S2,Prieto S1,Levi-Meyrueis C2,Zaragoza P1,Miroux B2,Ricquier D2,Bouillaud F2,Rial E1

Affiliation:

1. Centro de Investigaciones Biólogicas, C.S.I.C., Velázquez 144, 28006 Madrid, Spain

2. Centre de Recherche sur l'Endocrinologie Moláculaire et le Dáveloppement, C.N.R.S., 9 rue Jules Hetzel, 92190 Meudon, France

Abstract

The uncoupling protein (UCP) of brown adipose tissue is a regulated proton carrier which allows uncoupling of mitochondrial respiration from ATP synthesis and, therefore, dissipation of metabolic energy as heat. In this article we demonstrate that, when UCP is expressed in Saccharomyces cerevisiae, it retains all its functional properties: proton and chloride transport, high-affinity binding of nucleotides and regulation of proton conductance by nucleotides and fatty acids. Site-directed mutagenesis demonstrates that sequential replacement by serine of cysteine residues in the UCP does not affect either its uncoupling activity or its regulation by nucleotides and fatty acids, and therefore establishes that none of the seven cysteine residues present in the wild-type UCP is critical for its activity. These data indicate that transport models involving essential thiol groups can be discounted and that chemical modification data require critical re-evaluation.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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