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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >An internal targeting signal directing proteins into the mitochondrial intermembrane space
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An internal targeting signal directing proteins into the mitochondrial intermembrane space

机译：内部靶向信号将蛋白质导入线粒体膜间空间

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摘要

Import of most nucleus-encoded preproteins into mitochondria is mediated by N-terminal presequences and requires a membrane potential and ATP hydrolysis. Little is known about the chemical nature and localization of other mitochondrial targeting signals or of the mechanisms by which they facilitate membrane passage. Mitochondrial heme lyases lack N-terminal targeting information. These proteins are localized in the intermembrane space and are essential for the covalent attachment of heme to c type cytochromes. For import of heme lyases, the translocase of the mitochondrial outer membrane complex is both necessary and sufficient. Here, we report the identification of the targeting signal of mitochondrial heme lyases in the third quarter of these proteins. The targeting sequence is highly conserved among all known heme lyases. Its chemical character is hydrophilic because of a large fraction of both positively and negatively charged amino acid residues. These features clearly distinguish this signal from classical presequences. When inserted into a cytosolic protein, the targeting sequence directs the furion protein into the intermembrane space, even in the absence of a membrane potential or ATP hydrolysis. The heme lyase targeting sequence represents the intermembrane space and harbors two types of information. It as sures accurate recognition and translocation by the translocase of the mitochondrial outer membrane complex. and it is responsible for driving the import reaction by undergoing high-affinity interactions with components of the intermembrane space.
机译：N端的前序介导大多数核编码的前蛋白导入线粒体，需要膜电位和ATP水解。关于其他线粒体靶向信号的化学性质和定位或它们促进膜通过的机制知之甚少。线粒体血红素裂解酶缺乏N端靶向信息。这些蛋白质位于膜间空间中，对于血红素与c型细胞色素的共价结合至关重要。对于血红素裂解酶的导入，线粒体外膜复合物的转位酶既必要又充分。在这里，我们报告了在这些蛋白质的第三季度中线粒体血红素裂解酶的靶向信号的鉴定。靶向序列在所有已知的血红素裂解酶中高度保守。由于大部分带正电和带负电的氨基酸残基，其化学性质是亲水的。这些特征清楚地将该信号与经典序列区别开来。当插入胞质蛋白中时，即使在没有膜电位或ATP水解的情况下，靶向序列也可将先驱蛋白导入膜间空间。血红素裂解酶靶向序列代表膜间空间并包含两种类型的信息。可以肯定的是，线粒体外膜复合物的转位酶可以准确识别和转运。它通过与膜间空间的各组分进行高亲和力相互作用，来驱动导入反应。

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