The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex |
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Authors: | Franziska Lueder |
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Affiliation: | Department of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville 3010, Australia |
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Abstract: | The assembly of mitochondrial outer membrane proteins is an essential process, mediated by the SAM complex and a set of additional protein modules. We show that one of these, Mim1, is anchored in the outer membrane with its N-terminus exposed to the cytosol and its C-terminus in the mitochondrial intermembrane space. Using an in vitro assay to measure the multi-step pathway for assembly of Tom40 into the TOM complex, we find that an “early reaction” mediated by the SAM complex is regulated by the N-terminal domain of Mim1. In addition, a “late reaction” catalysed by the Sam37 subunit of the SAM complex is also influenced by Mim1. Thus, Mim1 participates at multiple stages in the assembly of the TOM complex. |
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Keywords: | Protein import β-Barrel protein Mitochondria SAM complex Outer membrane Membrane protein assembly |
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