The Journal of Cell Biology · 2011 · 148 citations · 49 references
Life SciencesBiochemistryMolecular BiologyIntracellular TransportMembrane BiochemistryMitochondrial BiologyMitochondrial BiogenesisMitochondrial MembranesMitochondrial Protein ImportMitochondrial TransportOrganelle BiologyOrganelle StructureImport Of Beta-barrel ProteinsMembrane Protein ImportMitochondrial Intermembrane Space ProteinsMitochondrial Protein Import MachineryOuter Membrane Protein InsertionOuter Membrane ProteinsTransmembrane HelicesTransmembrane Proteins
The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments.
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Structural Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20
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Machinery for protein sorting and assembly in the mitochondrial outer membrane
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