Interaction of mammalian mitochondrial ribosomes with the inner membrane

Interaction of mammalian mitochondrial ribosomes with the inner membrane
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DOI:
10.1074/jbc.m002173200
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发表时间:
2000-09-22
影响因子:
4.8
通讯作者:
Spremulli, L
Spremulli, L
中科院分区:
生物学2区
文献类型:
--
作者:
Liu, MQ;Spremulli, L

文献摘要

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动物线粒体蛋白质生物合成的所有产物都是定位于内膜的疏水性蛋白质。因此,这些蛋白质的合成可能发生在与内膜相关的核糖体上。为了检验这种可能性,使用rRNAs探针检查了牛线粒体的内膜和基质部分是否存在核糖体。有40%到50%的核糖体与内膜分离。与内膜相关的核糖体大约有一半可以在高盐处理下释放,这表明它们主要通过静电力与膜相互作用。用嘌呤霉素处理后没有观察到核糖体的释放,这表明观察到的联系不是由于新生的多肽链插入膜中所致。在Triton X-100存在的情况下,部分核糖体与膜的剩余部分一起保留,不能溶解。这些核糖体可能与膜上的大分子寡聚复合体有关。
All of the products of mitochondrial protein biosynthesis in animals are hydrophobic proteins that are localized in the inner membrane. Hence, it is possible that the synthesis of these proteins could occur on ribosomes associated with the inner membrane. To examine this possibility, inner membrane and matrix fractions of bovine mitochondria were examined for the presence of ribosomes using probes for the rRNAs. Between 40 and 50% of the ribosomes were found to fractionate with the inner membrane. About half of the ribosomes associated with the inner membrane could be released by high salt treatment, indicating that they interact with the membrane largely through electrostatic forces. No release of the ribosome was observed upon treatment with puromycin, suggesting that the association observed is not due to insertion of a nascent polypeptide chain into the membrane. A fraction of the ribosomes remained with residual portions of the membranes that cannot be solubilized in the presence of Triton X-100. These ribosomes may be associated with large oligomeric complexes in the membrane.