Open AccessCytoplasmically made subunits of yeast mitochondrial F1-ATPase and cytochrome c oxidase are synthesized as individual precursors, not as polyproteins.
Author(s) -
Alfred S. Lewin,
I Gregor,
Thomas L. Mason,
Nathan Nelson,
Gottfried Schatz
Publication year - 1980
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.7.3998
Subject(s) - cytochrome c oxidase , biochemistry , mitochondrion , yeast , oxidoreductase , protein subunit , organelle , electron transport complex iv , cytochrome c , enzyme , chemistry , oxidase test , biology , microbiology and biotechnology , gene
At least three subunits of yeast mitochondrial F1-ATPase (ATP phosphohydrolase, EC 3.6.1.3) and at least two subunits of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) are synthesized outside the mitochondria and imported into the organelles as individual precursors that are between 2000 and 6000 daltons larger than the mature subunits. These precursors were shown to be primary translation products. Therefore, neither the five F1 subunits nor the four small cytochrome c oxidase subunits are synthesized as a single polyprotein.
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