Author:
Busto Jon V.,Mathar Hannah,Steiert Conny,Schneider Eva F.,Straub Sebastian P.,Ellenrieder Lars,Song Jiyao,Stiller Sebastian B.,Lübbert Philipp,Guiard Bernard,den Brave Fabian,Schulte Uwe,Fakler Bernd,Becker Thomas,Wiedemann Nils
Abstract
SUMMARYThe majority of mitochondrial precursor proteins are imported through the Tom40 β-barrel channel of the translocase of the outer membrane (TOM). The sorting and assembly machinery (SAM) is essential for β-barrel membrane protein insertion into the outer membrane and thus required for the assembly of the TOM complex. Here we demonstrate that the a-helical outer membrane protein Mco6 forms a complex with the mitochondrial distribution and morphology protein Mdm10 as part of the SAM machinery. Moreover, Mco6 also interacts with the subunit Mim1 of the mitochondrial import complex (MIM), which is itself required for the biogenesis of a-helical outer membrane proteins.MCO6andMDM10display a negative genetic interaction and aMCO6-MDM10yeast double mutant contains reduced levels of TOM complex. Cells lacking Mco6 affect the levels of Mdm10 and MIM-subunits associated with assembly defects of the TOM complex. Thus, this work reveals a role of the SAMMco6complex for the biogenesis of the mitochondrial outer membrane.
Publisher
Cold Spring Harbor Laboratory
Cited by
1 articles.
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