| Literature DB >> 2905264 |
M Yang1, R E Jensen, M P Yaffe, W Oppliger, G Schatz.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1988 PMID: 2905264 PMCID: PMC454964 DOI: 10.1002/j.1460-2075.1988.tb03271.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598