Yang M, Jensen R E, Yaffe M P, Oppliger W, Schatz G
Biocenter, University of Basel, Switzerland.
EMBO J. 1988 Dec 1;7(12):3857-62. doi: 10.1002/j.1460-2075.1988.tb03271.x.
We have purified the metalloprotease which is localized in the soluble matrix space of Saccharomyces cerevisiae mitochondria and cleaves the amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins. The enzyme consists of two loosely associated non-identical subunits of mol. wt 48,000 and 51,000, respectively. Attempts to separate the two subunits from each other caused loss of activity. The smaller subunit had been identified as the product of the nuclear MAS1 gene (Witte et al., 1988). The larger subunit is now identified as the product of the nuclear MAS2 gene.
我们已经纯化了一种金属蛋白酶,该酶定位于酿酒酵母线粒体的可溶性基质空间中,可从导入的线粒体前体蛋白上切割氨基末端的基质靶向序列。该酶由两个分子量分别为48,000和51,000的松散结合的不同亚基组成。试图将这两个亚基彼此分离会导致活性丧失。较小的亚基已被鉴定为核MAS1基因的产物(维特等人,1988年)。现在,较大的亚基被鉴定为核MAS2基因的产物。