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J. Biol. Chem., Vol. 258, Issue 6, 3427-3430, 03, 1983
SM Gasser and G Schatz
The yeast mitochondrial outer membrane contains a major 29-kilodalton
protein which is encoded in the nucleus. When this polypeptide is
synthesized in vitro and then incubated with isolated yeast mitochondria,
it binds to the organelles and becomes resistant to externally added
trypsin. Post-translational insertion of the 29- kilodalton protein in
vitro is not accompanied by NH2-terminal processing, appears to require
neither ATP nor a transmembrane electrochemical potential, and is also
observed with purified outer membranes, but not with yeast microsomes. In
vitro insertion of the 29- kilodalton polypeptide is thus in several
respects different from that of polypeptides destined for the internal
compartments of the mitochondrion.
Import of proteins into mitochondria. In vitro studies on the biogenesis of the outer membrane
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