TRANSPORT OF PROTEINS INTO MITOCHONDRIA - TRANSLOCATIONAL INTERMEDIATES SPANNING CONTACT SITES BETWEEN OUTER AND INNER MEMBRANES
TRANSPORT OF PROTEINS INTO MITOCHONDRIA - TRANSLOCATIONAL INTERMEDIATES SPANNING CONTACT SITES BETWEEN OUTER AND INNER MEMBRANES
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DOI：
10.1016/0092-8674(85)90039-x
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发表时间：
1985-01-01
期刊：
影响因子：
64.5
通讯作者：
NEUPERT, W
中科院分区：
文献类型：
--
作者：
SCHLEYER, M;NEUPERT, W
ATP酶F1 β的前体蛋白质的易位中间体亚基和细胞色素C1跨线粒体膜使用两种不同的方法进行分析，低温下的运输和前体蛋白与抗体结合后的运输。在这两种条件下，前体部分运输到线粒体中的能量依赖性的方式。它们被基质中的金属蛋白酶加工，但大部分多肽链仍然存在于线粒体外膜的外表面。我们的结论是，前体转移到内膜或基质空间发生通过“易位接触位点”，前体多肽到F1 β。和细胞色素C1首先进入氨基末端的基质空间;氨基末端“结构域样”结构上的跨膜运动需要膜电位，但完成多肽的主要部分的移位不需要膜电位。
Translocation intermediates of precursor proteins of ATPase F1.beta. subunit and cytochrome c1 across mitochondrial membranes were analyzed using two different approaches, transport at low temperature and transport after binding of precursor proteins to antibodies. Under both conditions precursors were partially transported into mitochondria in an energy-dependent manner. They were processed by the metalloprotease in the matrix but a major proportion of the polypeptide chains was still present at the outer face of the outer mitochondrial membrane. We conclude that transfer of precursors into the inner membrane or matrix space occurs through "translocation contact sites"; precursor polypeptides to F1.beta. and cytochrome c1 enter the matrix space with the amino terminus first; and a membrane potential is required for the transmembrane movement on an amino-terminal "domain-like: structure but not for completing translocation of the major part of the polypeptides.