Premium
A yeast mutant temperature‐sensitive for mitochondrial assembly is deficient in a mitochondrial protease activity that cleaves imported precursor polypeptides.
Author(s) -
Yaffe M.P.,
Ohta S.,
Schatz G.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb03893.x
Subject(s) - biology , mutant , yeast , protease , mitochondrion , mitochondrial dna , biochemistry , saccharomyces cerevisiae , microbiology and biotechnology , enzyme , gene
We have previously described two yeast mutants which, at elevated temperature, stop growing and accumulate precursors to several imported mitochondrial proteins. We now show that one of these mutants (mas 1) is deficient in a matrix‐located protease activity which cleaves the pre‐sequences from mitochondrial precursor proteins. Isolated mas 1 mitochondria catalyze oxidative phosphorylation, exhibit respiratory control and import mitochondrial precursor polypeptides, but are defective in removing transient pre‐sequences from imported precursors. The phenotype of the mas 1 mutant suggests that the matrix‐located processing protease is essential for growth and for mitochondrial assembly.