Koehler C M, Jarosch E, Tokatlidis K, Schmid K, Schweyen R J, Schatz G
Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Science. 1998 Jan 16;279(5349):369-73. doi: 10.1126/science.279.5349.369.
In order to reach the inner membrane of the mitochondrion, multispanning carrier proteins must cross the aqueous intermembrane space. Two essential proteins of that space, Tim10p and Tim12p, were shown to mediate import of multispanning carriers into the inner membrane. Both proteins formed a complex with the inner membrane protein Tim22p. Tim10p readily dissociated from the complex and was required to transport carrier precursors across the outer membrane; Tim12p was firmly bound to Tim22p and mediated the insertion of carriers into the inner membrane. Neither protein was required for protein import into the other mitochondrial compartments. Both proteins may function as intermembrane space chaperones for the highly insoluble carrier proteins.
为了抵达线粒体的内膜,多跨膜载体蛋白必须穿过水相的膜间隙。该间隙中的两种重要蛋白质Tim10p和Tim12p被证明可介导多跨膜载体导入内膜。这两种蛋白质都与内膜蛋白Tim22p形成复合物。Tim10p很容易从复合物中解离,并且是载体前体穿过外膜所必需的;Tim12p则牢固地结合在Tim22p上,并介导载体插入内膜。这两种蛋白质都不是蛋白质导入其他线粒体区室所必需的。这两种蛋白质都可能作为高度不溶性载体蛋白的膜间隙伴侣发挥作用。