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酵母线粒体纯化的内膜蛋白酶I是一种异源二聚体。

Purified inner membrane protease I of yeast mitochondria is a heterodimer.

作者信息

Schneider A, Oppliger W, Jenö P

机构信息

Biozentrum, University of Basel, Switzerland.

出版信息

J Biol Chem. 1994 Mar 25;269(12):8635-8.

PMID:8132591
Abstract

Inner membrane protease I is bound to the outer face of the yeast mitochondrial inner membrane and mediates the proteolytic maturation of cytochrome b2 and cytochrome oxidase subunit II. We have previously shown that one of its subunits is a 21.4-kDa integral membrane protein encoded by the nuclear IMP1 gene. We have now purified the active protease approximately 300-fold from yeast mitochondria. It has an apparent molecular weight of 35,000 and contains not only Imp1p but also a previously unrecognized 19-kDa subunit. Partial amino acid sequencing identifies this subunit as the product of the recently described IMP2 gene (Nunnari, J., Fox, T., and Walter, P. (1993) Science 262, 1997-2004).

摘要

内膜蛋白酶I与酵母线粒体内膜的外表面结合,并介导细胞色素b2和细胞色素氧化酶亚基II的蛋白水解成熟。我们之前已经表明,它的一个亚基是由核基因IMP1编码的21.4 kDa整合膜蛋白。我们现在已经从酵母线粒体中纯化出活性蛋白酶,纯化倍数约为300倍。它的表观分子量为35,000,不仅含有Imp1p,还含有一个以前未被识别的19 kDa亚基。部分氨基酸测序确定该亚基为最近描述的IMP2基因的产物(Nunnari, J., Fox, T., and Walter, P. (1993) Science 262, 1997 - 2004)。

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