Journal
CELL REPORTS
Volume 31, Issue 4, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.107567
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- Deutsche Forschungsgemeinschaft (DFG) [Sonderforschungsbereich 746, BE 4679/2-2, PF 202/9-1, 278002225/RTG 2202, 390939984]
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The mitochondrial outer membrane contains integral proteins with alpha-helical membrane anchors or a transmembrane beta-barrel. The translocase of the outer membrane (TOM) cooperates with the sorting and assembly machinery (SAM) in the import of beta-barrel proteins, whereas the mitochondrial import (MIM) complex inserts precursors of multi-spanning alpha-helical proteins. Single-spanning proteins constitute more than half of the integral outer membrane proteins; however, their biogenesis is poorly understood. We report that the yeast MIM complex promotes the insertion of proteins with N-terminal (signal-anchored) or C-terminal (tail-anchored) membrane anchors. The MIM complex exists in three dynamic populations. MIM interacts with TOM to accept precursor proteins from the receptor Tom70. Free MIM complexes insert single-spanning proteins that are imported in a Tom70-independent manner. Finally, coupling of MIM and SAM promotes early assembly steps of TOM subunits. We conclude that the MIM complex is a major and versatile protein translocase of the mitochondrial outer membrane.
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