Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon
Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon
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DOI：
10.1126/science.274.5284.103
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发表时间：
1996-10-04
期刊：
影响因子：
56.9
通讯作者：
Suzuki, CK
中科院分区：
文献类型：
--
作者：
Rep, M;vanDijl, JM;Suzuki, CK
Afg3p和Rca1p是酵母线粒体中依赖三磷酸腺苷（ATP）的金属蛋白酶。缺乏这两种蛋白质的细胞表现出呼吸依赖性生长、细胞内合成蛋白质的降解和内膜复合物的组装的缺陷。缺陷的生长和蛋白质组装，但不是在降解，被抑制酵母线粒体Lon，ATP依赖性丝氨酸蛋白酶的过度生产。Lon的抑制作用通过蛋白水解位点的失活而增强，并通过ATP结合位点的突变而被阻止。有人建议，线粒体蛋白酶Lon，Afg3p和Rca1p也可以在线粒体蛋白质复合物的组装中起到伴侣样功能。
Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.