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External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica

雅罗维亚 生物 氧化还原酶 线粒体内膜 NADH脱氢酶 电子传递复合体Ⅰ 线粒体 生物化学 蛋白质亚单位 内膜 电化学梯度 呼吸链 线粒体基质 泛醇 酿酒酵母 胞浆 细胞生物学 酵母 辅酶Q-细胞色素c还原酶 基因 细胞色素c
作者
Stefan Kerscher,Andrea Eschemann,Pamela M. Okun,Ulrich Brandt
出处
期刊:Journal of Cell Science [The Company of Biologists]
卷期号:114 (21): 3915-3921 被引量:52
标识
DOI:10.1242/jcs.114.21.3915
摘要

Alternative NADH:ubiquinone oxidoreductases are single subunit enzymes capable of transferring electrons from NADH to ubiquinone without contributing to the proton gradient across the respiratory membrane. The obligately aerobic yeast Yarrowia lipolytica has only one such enzyme, encoded by the NDH2 gene and located on the external face of the mitochondrial inner membrane. In sharp contrast to ndh2 deletions, deficiencies in nuclear genes for central subunits of proton pumping NADH:ubiquinone oxidoreductases (complex I) are lethal. We have redirected NDH2 to the internal face of the mitochondrial inner membrane by N-terminally attaching the mitochondrial targeting sequence of NUAM, the largest subunit of complex I. Lethality of complex I mutations was rescued by the internal, but not the external version of alternative NADH:ubiquinone oxidoreductase. Internal NDH2 also permitted growth in the presence of complex I inhibitors such as 2-decyl-4-quinazolinyl amine (DQA). Functional expression of NDH2 on both sides of the mitochondrial inner membrane indicates that alternative NADH:ubiquinone oxidoreductase requires no additional components for catalytic activity. Our findings also demonstrate that shuttle mechanisms for the transfer of redox equivalents from the matrix to the cytosolic side of the mitochondrial inner membrane are insufficient in Y. lipolytica.
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