A single mutation in uncoupling protein of rat brown adipose tissue mitochondria abolishes GDP sensitivity of H+ transport.

摘要: The uncoupling protein is one of a family mitochondrial transport proteins involved in energy metabolism. It dissipates oxidative to generate heat, either by catalyzing proton directly or fatty acid anion transport, thus enabling acids act as cycling protonophores. This process tightly regulated purine nucleotides. We have expressed yeast and examined its activity after reconstitution into proteoliposomes. A directed change Arg276 Leu Gln completely abolished nucleotide inhibition protonophoretic action the reconstituted mutant without affecting process. first residue functional importance be identified protein. Mutation homologous ADP/ATP translocator prevented growth on nonfermentable carbon source, presumably interfering with exchange (Nelson, D. R., Lawson, J. E., Klingenberg, M., Douglas, M. G. (1993) Mol. Biol. 230, 1159-1170). Demonstration essential role single protein-nucleotide interaction within these two transporters direct evidence that belong same gene family.