Koehler C M, Leuenberger D, Merchant S, Renold A, Junne T, Schatz G
Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2141-6. doi: 10.1073/pnas.96.5.2141.
The human deafness dystonia syndrome results from the mutation of a protein (DDP) of unknown function. We show now that DDP is a mitochondrial protein and similar to five small proteins (Tim8p, Tim9p, Tim10p, Tim12p, and Tim13p) of the yeast mitochondrial intermembrane space. Tim9p, Tim10p, and Tim12p mediate the import of metabolite transporters from the cytoplasm into the mitochondrial inner membrane and interact structurally and functionally with Tim8p and Tim13p. DDP is most similar to Tim8p. Tim8p exists as a soluble 70-kDa complex with Tim13p and Tim9p, and deletion of Tim8p is synthetically lethal with a conditional mutation in Tim10p. The deafness dystonia syndrome thus is a novel type of mitochondrial disease that probably is caused by a defective mitochondrial protein-import system.
人类耳聋肌张力障碍综合征是由一种功能未知的蛋白质（DDP）突变引起的。我们现在发现DDP是一种线粒体蛋白，与酵母线粒体内膜间隙的五种小蛋白（Tim8p、Tim9p、Tim10p、Tim12p和Tim13p）相似。Tim9p、Tim10p和Tim12p介导代谢物转运体从细胞质导入线粒体内膜，并在结构和功能上与Tim8p和Tim13p相互作用。DDP与Tim8p最为相似。Tim8p与Tim13p和Tim9p以可溶性70 kDa复合物的形式存在，Tim8p的缺失与Tim10p中的条件性突变具有合成致死性。因此，耳聋肌张力障碍综合征是一种新型的线粒体疾病，可能由有缺陷的线粒体蛋白质导入系统引起。
