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J. Biol. Chem., Vol. 276, Issue 21, 17679-17685, May 25, 2001
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From the Translocation of preproteins across the
mitochondrial outer membrane is mediated by the translocase of the
outer mitochondrial membrane (TOM) complex. We report the
molecular identification of Tom6 and Tom7, two small subunits of the
TOM core complex in the fungus Neurospora crassa.
Cross-linking experiments showed that both proteins were found to be in
direct contact with the major component of the pore, Tom40. In
addition, Tom6 was observed to interact with Tom22 in a manner that
depends on the presence of preproteins in transit. Precursors of both
proteins are able to insert into the outer membrane in
vitro and are assembled into authentic TOM complexes. The
insertion pathway of these proteins shares a common binding site with
the general import pathway as the assembly of both Tom6 and Tom7 was
competed by a matrix-destined precursor protein. This assembly was
dependent on the integrity of receptor components of the TOM machinery
and is highly specific as in vitro-synthesized yeast Tom6
was not assembled into N. crassa TOM complex. The targeting
and assembly information within the Tom6 sequence was found to be
located in the transmembrane segment and a flanking segment toward the
N-terminal, cytosolic side. A hybrid protein composed of the C-terminal
domain of yeast Tom6 and the cytosolic domain of N. crassa
Tom6 was targeted to the mitochondria but was not taken up into TOM
complexes. Thus, both segments are required for assembly into the TOM
complex. A model for the topogenesis of the small Tom subunits is discussed.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF321882 and AF321883.
Assembly of Tom6 and Tom7 into the TOM Core Complex of
Neurospora crassa*
,,, and
Institut für Physiologische Chemie der
Universität München, 80336 München, Germany,
§ Department of Biological Sciences, University of Alberta,
Edmonton, Alberta T6G 2E9, Canada, and ¶ Department of
Biochemistry, The Hebrew University, Hadassah Medical School, Jerusalem
91120, Israel
*
This work was supported in part by grants of the
Sonderforschungsbereich 184 of the Deutsche Forschungsgemeinschaft, the
Fonds der Chemischen Industrie, and the Medical Research Council of Canada (to F. E. N.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
972-2-6758292; Fax: 972-2-6757379; E-mail:
rapaportd@md.huji.ac.il.
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