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Apocytochrome c follows a unique pathway into
mitochondria. Import does not require the general protein translocation
machinery, protease-sensitive components of the outer membrane, or a
membrane potential across the inner membrane. We investigated the
membrane binding and translocation steps of the import reaction using
purified outer membrane vesicles (OMV) from Neurospora crassa mitochondria. OMV specifically bound, but did not import
apocytochrome c. If, however, specific antibodies were
enclosed inside OMV, apocytochrome c was accumulated in
soluble form in the lumen. Import was reversible, since apocytochrome
c became accessible to external protease after release from
the antibodies. Thus, OMV are competent of translocating apocytochrome
c into their lumen, but lack a binding partner which traps the
apoprotein. In intact mitochondria, cytochrome c heme lyase
(CCHL), a peripheral protein of the inner membrane, serves such a
function by stably associating with apocytochrome c in a
complex which is detectable by co-immunoprecipitation. We suggest a
model for the import mechanism of apocytochrome c in which the
apoprotein specifically associates with and reversibly passes across
the outer membrane. Translocation is rendered unidirectional by stable
association with CCHL which serves as a ``trans side
receptor.'' Finally, heme is attached by CCHL and the holoprotein
folds into its native structure.
Volume 270,
Number 21,
Issue of May 26, pp. 12390-12397, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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