Spannagel C, Vaillier J, Arselin G, Graves P V, Grandier-Vazeille X, Velours J
Institut de Biochimie et Génétique Cellulaires du CNRS, Université Victor Ségalen, Bordeaux II, 1 rue Camille Saint Saëns, 33077 Bordeaux Cedex, France.
Biochim Biophys Acta. 1998 Nov 11;1414(1-2):260-4. doi: 10.1016/s0005-2736(98)00174-6.
Yeast mitochondria having either the D54C or E55C mutations in subunit 4 (subunit b), which is a component of the ATP synthase stator, displayed a spontaneous disulfide bridge between two subunits 4. This dimer was not soluble upon Triton X-100 extraction either at concentrations which extract the yeast ATP synthase or at higher concentrations. Increasing detergent concentrations led to a lack of the oligomycin-sensitive ATPase activity, thus showing an uncoupling between the two sectors of the mutated enzymes due to the dissociation of the subunit 4 dimer from the mutant enzyme. There is only one subunit 4 (subunit b) per eukaryotic ATP synthase. As a consequence, the results are interpreted as the proximity of ATP synthase complexes within the inner mitochondrial membrane.
在ATP合酶定子组件亚基4（亚基b）中具有D54C或E55C突变的酵母线粒体，在两个亚基4之间显示出自发形成的二硫键。无论是在能够提取酵母ATP合酶的浓度下，还是在更高浓度下，用Triton X-100提取时，这种二聚体都不溶解。增加去污剂浓度会导致寡霉素敏感的ATP酶活性丧失，从而表明由于突变酶的亚基4二聚体解离，突变酶的两个部分之间发生了解偶联。每个真核生物ATP合酶只有一个亚基4（亚基b）。因此，这些结果被解释为线粒体内膜内ATP合酶复合物的接近。
