Reference: Lueder F and Lithgow T (2009) The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex. FEBS Lett 583(9):1475-80

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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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Journal Article | Research Support, Non-U.S. Gov't
Authors
Lueder F, Lithgow T
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