
pmid: 7600576
We have identified a complex in mitochondria that functions as a part of the preprotein import machinery of the inner membrane (MIM complex). Two known components, MIM23 and MIM17, and two novel components, MIM33 and MIM14, were found as constituents of this complex. In the presence of a translocating chain, the outer membrane import machinery (MOM complex) and the MIM complex form translocation contact sites. On the matrix side, the MIM complex is associated with the mt-Hsp70-MIM44 system. We propose a structure of the import machinery in which the MIM complex constitutes a proteinaceous channel that accepts preproteins from the MOM complex, facilitates their reversible transmembrane movement, and mediates unidirectional transport by linkage to the ATP-dependent mt-Hsp70-MIM44 system.
Base Sequence, Biochemistry, Genetics and Molecular Biology(all), Molecular Sequence Data, Membrane Proteins, Membrane Transport Proteins, Intracellular Membranes, Mitochondrial Membrane Transport Proteins, Polymerase Chain Reaction, Mitochondria, Fungal Proteins, Repressor Proteins, Adenosine Triphosphate, Mitochondrial Precursor Protein Import Complex Proteins, Escherichia coli, HSP70 Heat-Shock Proteins, Cloning, Molecular, Genome, Fungal, Protein Precursors, Carrier Proteins, Protein Processing, Post-Translational, DNA Primers
Base Sequence, Biochemistry, Genetics and Molecular Biology(all), Molecular Sequence Data, Membrane Proteins, Membrane Transport Proteins, Intracellular Membranes, Mitochondrial Membrane Transport Proteins, Polymerase Chain Reaction, Mitochondria, Fungal Proteins, Repressor Proteins, Adenosine Triphosphate, Mitochondrial Precursor Protein Import Complex Proteins, Escherichia coli, HSP70 Heat-Shock Proteins, Cloning, Molecular, Genome, Fungal, Protein Precursors, Carrier Proteins, Protein Processing, Post-Translational, DNA Primers
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