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(Received for publication, August 8, 1996, and in revised form, December 5, 1996)
From the The
Volume 272, Number 9,
Issue of February 28, 1997
pp. 6044-6050
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and
Service de Neurobiologie Physico-Chimique,
Centre National de la Recherche Scientifique, Unité Propre de
Recherche 9071, Institut de Biologie Physico-Chimique, 13 rue P. et M. Curie, 75005 Paris, France and the 
Laboratoire de Neurobiologie
Cellulaire et Moléculaire, Centre National de la Recherche
Scientifique, 91198 Gif-sur-Yvette Cedex, France
eptide-
ensitive
hannel (PSC), a cationic channel of the mitochondrial
outer membrane, is blocked by synthetic mitochondrial presequences and
by nonmitochondrial basic peptides such as dynorphin B(1-13). Both
types of peptides are imported into mitochondria. However, the import
of dynorphin B(1-13) had to be further characterized since its
properties differed from those of the general import pathway used by
mitochondrial peptides. Cross-linking experiments with iodinated
dynorphin B(1-13) led to the labeling of TOM 40/ISP 42, a component of
the protein import machinery of the outer membrane. Accordingly,
dynorphin B(1-13) could also be used as a presequence to direct the
import of a cytosolic protein into the mitochondria. Pretreatment of
intact mitochondria by trypsin removed components capable of
discriminating between true mitochondrial presequences and other basic
peptides active on the PSC. After proteolysis, both types of peptides
appeared to cross the outer membrane through the same pathway.
Involvement of the PSC in the translocation complex was shown by
immunoprecipitation of the PSC activity by anti-ISP 42 antibodies.
Taken together, the present data reinforce the hypothesis that the PSC
is the pore responsible for the translocation of protein through the
outer membrane.
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