PHOSPHODIESTER BOND-CLEAVAGE OUTSIDE MITOCHONDRIA IS REQUIRED FOR THE COMPLETION OF PROTEIN IMPORT INTO THE MITOCHONDRIAL MATRIX
PHOSPHODIESTER BOND-CLEAVAGE OUTSIDE MITOCHONDRIA IS REQUIRED FOR THE COMPLETION OF PROTEIN IMPORT INTO THE MITOCHONDRIAL MATRIX
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DOI：
10.1016/0092-8674(87)90541-1
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发表时间：
1987-06-05
期刊：
影响因子：
64.5
通讯作者：
DOUGLAS, MG
中科院分区：
文献类型：
--
作者：
CHEN, WJ;DOUGLAS, MG
目前的研究表明，磷酸二酯键（最可能是ATP）的水解是完成F1-ATP酶β-ATP酶的输入所需的独特的第二步。进入线粒体。该步骤遵循膜电位依赖性第一步骤。我们显示，使用腺嘌呤核苷酸转运的抑制剂和类似物β，伽马AMP-PCP，这种磷酸二酯水解依赖性完成蛋白质输入所需的活性位于线粒体内膜外。这种活性被认为作用于易位位点的前体，使其感受态或催化其直接通过输入装置的矢量运动。这种活性共享归因于热休克家族的蛋白质的性质，其被提议参与部分变性蛋白质和新生肽的ATP依赖性重折叠。
The present studies show that hydrolysis of a phosphodiester bond, most likely ATP, is a distinct, second step required to complete import of the F1-ATPase .beta.-subunit into the mitochondria. This step follows a membrane potential-dependent first step. We show, using an inhibitor of adenine nucleotide transport and the analogue .beta.,.gamma.-AMP-PCP, that the activity required for this phosphodiester hydrolysis-dependent completion of protein import resides outside the mitochondrial inner membrane. This activity is proposed to act on the precursor at the site of translocation either to render it competent or to catalyze its vectorial movement directly through the import apparatus. This activity shares properties ascribed to proteins of the heat-shock family, which are proposed to participate in the ATP-dependent refolding of partially denatured proteins and nascent peptides.