Zwizinski C, Schleyer M, Neupert W
J Biol Chem. 1984 Jun 25;259(12):7850-6.
Mild trypsin treatment of isolated Neurospora mitochondria strongly inhibits their ability to bind and import the precursors of several mitochondrial proteins. Evidence is presented for two proteins, the ADP/ATP carrier and the mitochondrial porin, that specific binding of the precursors to the outer surface of the mitochondria is affected by the protease treatment. We suggest that the receptors that mediate the import of these two precursors are proteinaceous. Treatment of mitochondria with elastase also inhibits the binding and import of the ADP/ATP carrier and the porin. In contrast the import of the precursors of subunits 2 and 9 of the mitochondrial proton-translocating ATPase was unaffected by elastase treatment at the concentrations used. We suggest that the import pathways of the latter two proteins are distinct from those of the ADP/ATP carrier and the porin.
用温和的胰蛋白酶处理分离得到的粗糙脉孢菌线粒体，会强烈抑制其结合和导入几种线粒体蛋白前体的能力。有证据表明，对于两种蛋白，即ADP/ATP载体和线粒体孔蛋白，蛋白酶处理会影响前体与线粒体外表面的特异性结合。我们认为介导这两种前体导入的受体是蛋白质性质的。用弹性蛋白酶处理线粒体也会抑制ADP/ATP载体和孔蛋白的结合与导入。相比之下，在所使用的浓度下，弹性蛋白酶处理不会影响线粒体质子转运ATP酶亚基2和亚基9前体的导入。我们认为后两种蛋白的导入途径与ADP/ATP载体和孔蛋白的导入途径不同。
