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J. Biol. Chem., Vol. 269, Issue 16, 11893-11901, 04, 1994
J Schlossmann, K Dietmeier, N Pfanner and W Neupert
The import receptor MOM72 constitutes part of the protein translocation
machinery of the outer mitochondrial membrane, the receptor-general
insertion pore complex. The protein contains a membrane anchor at the NH2
terminus and a large cytosolic domain. In yeast and Neurospora crassa the
cytosolic domain comprises about 570-580 amino acid residues. The cytosolic
domain of yeast MOM72 was purified after expression in Escherichia coli as
a homogeneous monomeric protein. It can recognize precursor proteins as
demonstrated by its ability to compete for binding and import into the
mitochondria and to physically interact with preproteins. A subset of
preproteins including the ADP/ATP carrier and the phosphate carrier
interact with very high affinity, precursors that are known to be targeted
via MOM72. Thus, the cytosolic domain of MOM72 plays a critical function in
the recognition of preproteins by directly binding to precursor proteins
and thereby facilitating their targeting to mitochondria.
Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72
Institut fur Physiologische Chemie, Universitat Munchen, Germany.
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