A mitochondrial protease with two catalytic subunits of nonoverlapping specificities.

A mitochondrial protease with two catalytic subunits of nonoverlapping specificities.
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一种线粒体蛋白酶,具有两个特异性不重叠的催化亚基。

DOI:
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发表时间:
1993
期刊:
影响因子:
56.9
通讯作者:
Peter Walter
Peter Walter
中科院分区:
综合性期刊1区
文献类型:
--
作者:
J. Nunnari;T. Fox;Peter Walter

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The mitochondrial inner membrane protease is required for the maturation of mitochondrial proteins that are delivered to the intermembrane space. In the yeast Saccharomyces cerevisiae, this protease is now shown to be a complex that contains two catalytic subunits, Imp2p and the previously identified Imp1p. Primary structure similarity indicates that Imp1p and Imp2p are related to each other and to the family of eubacterial and eukaryotic signal peptidases. Imp1p and Imp2p have separate, nonoverlapping substrate specificities. In addition to its catalyzing the cleavage of intermembrane space sorting signals, Imp2p is required for the stable and functional expression of Imp1p. Thus, inner membrane protease, and by analogy eukaryotic multisubunit signal peptidases, may have acquired multiple catalytic subunits by gene duplication to broaden their range of substrate specificity.
内膜蛋白酶 I,一种在酵母中介导线粒体内蛋白质分选的酶。
DOI: 10.1002/j.1460-2075.1991.tb07944.x
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影响因子: --
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DOI: --
发表时间: 1989
期刊: The Journal of biological chemistry
影响因子: --
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DOI: 10.1073/pnas.83.3.581
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