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(Received for publication, April 22, 1997, and in revised form, June 5, 1997)
From the Institut für Biochemie und Molekularbiologie,
Universität Freiburg, Hermann-Herder-Straße 7, D-79104 Freiburg, Germany
The preprotein translocase of the outer
mitochondrial membrane (Tom) is a multi-subunit complex required for
specific recognition and membrane translocation of nuclear-encoded
preproteins. We have expressed and purified the cytosolic domains of
three postulated import receptors, Tom20, Tom22, and Tom70. Each
receptor domain is able to bind mitochondrial preproteins but with
different specificity. Tom20 binds both preproteins with N-terminal
presequences and preproteins with internal targeting signals; the
binding is enhanced by the addition of salt. Tom22 selectively
recognizes presequence-carrying preproteins in a salt-sensitive manner.
Tom70 preferentially binds preproteins with internal targeting
information. A chemically synthesized presequence peptide competes with
preproteins for binding to Tom20 and Tom22 but not to Tom70. We
conclude that each of the three import receptors binds preproteins
independently and by a different mechanism. Both Tom20 and Tom22
function as presequence receptors.
Volume 272, Number 33,
Issue of August 15, 1997
pp. 20730-20735
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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