The bulk of UCP3 expressed in yeast cells is incompetent for a nucleotide regulated H+ transport

被引：35

作者：

Heidkaemper, D

Winkler, E

Müller, V

Frischmuth, K

Liu, QY

Caskey, T

Klingenberg, M

机构：

[1] Univ Munich, Inst Phys Biochem, D-80336 Munich, Germany

[2] Merck & Co Inc, West Point, PA 19486 USA

来源：

FEBS LETTERS | 2000年 / 480卷 / 2-3期

关键词：

uncoupling protein; mitochondria; Saccharomyces cerevisiae; H+-transport; membrane potential; oxidative phosphorylation;

D O I：

10.1016/S0014-5793(00)01949-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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, mud 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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：265 / 270

页数：6

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