期刊
CELL
卷 154, 期 3, 页码 596-608出版社
CELL PRESS
DOI: 10.1016/j.cell.2013.06.033
关键词
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资金
- Deutsche Forschungsgemeinschaft
- Sonderforschungsbereich [746]
- Excellence Initiative of the German Federal and State Governments [EXC 294 BIOSS]
The mitochondrial outer membrane harbors two protein translocases that are essential for cell viability: the translocase of the outer mitochondrial membrane (TOM) and the sorting and assembly machinery (SAM). The precursors of beta-barrel proteins use both translocases-TOM for import to the intermembrane space and SAM for export into the outer membrane. It is unknown if the translocases cooperate and where the beta-barrel of newly imported proteins is formed. We established a position-specific assay for monitoring beta-barrel formation in vivo and in organello and demonstrated that the beta-barrel was formed and membrane inserted while the precursor was bound to SAM. beta-barrel formation was inhibited by SAM mutants and, unexpectedly, by mutants of the central import receptor, Tom22. We show that the cytosolic domain of Tom22 links TOM and SAM into a supercomplex, facilitating precursor transfer on the intermembrane space side. Our study reveals receptor-mediated coupling of import and export translocases as a means of precursor channeling.
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