Premium
The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H + transport
Author(s) -
Heidkaemper Dörthe,
Winkler Edith,
Müller Veronika,
Frischmuth Karina,
Liu Quingyun,
Caskey Thomas,
Klingenberg Martin
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01949-9
Subject(s) - ucp3 , uncoupling protein , oxidative phosphorylation , mitochondrion , yeast , biochemistry , chemistry , thermogenin , uncoupling agents , microbiology and biotechnology , intracellular , atp synthase , biology , gene , thermogenesis , brown adipose tissue , adipose tissue
The impact of uncoupling protein (UCP) 1, UCP3 and UCP3s expressed in yeast on oxidative phosphorylation, membrane potential and H + transport is determined. Intracellular ATP synthesis is inhibited by UCP3, much more than by UCP1, while similar levels of UCP3 and UCP1 exist in the mitochondrial fractions. Measurements of membrane potential and H + efflux in isolated mitochondria show that, different from UCP1, with UCP3 and UCP3s there is a priori a preponderant uncoupling not inhibited by GDP. The results are interpreted to show that UCP3 and UCP3s in yeast mitochondria are in a deranged state causing uncontrolled uncoupling, which does not represent their physiological function.