Journal
EMBO JOURNAL
Volume 29, Issue 17, Pages 2875-2887Publisher
WILEY
DOI: 10.1038/emboj.2010.149
Keywords
intermembrane space; mitochondria; phospholipid metabolism; protein import; yeast
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Funding
- NIGMS NIH HHS [R01 GM089853, R01 GM084015] Funding Source: Medline
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Ups1p, Ups2p, and Ups3p are three homologous proteins that control phospholipid metabolism in the mitochondrial intermembrane space (IMS). The Ups proteins are atypical IMS proteins in that they lack the two major IMS-targeting signals, bipartite presequences and cysteine motifs. Here, we show that Ups protein import is mediated by another IMS protein, Mdm35p. In vitro import assays show that import of Ups proteins requires Mdm35p. Loss of Mdm35p led to a decrease in steady state levels of Ups proteins in mitochondria. In addition, mdm35 Delta cells displayed a similar phenotype to ups1 Delta ups2 Delta ups3 Delta cells. Interestingly, unlike typical import machineries, Mdm35p associated stably with Ups proteins at a steady state after import. Demonstrating that Mdm35p is a functional component of Ups-Mdm35p complexes, restoration of Ups protein levels in mdm35 Delta mitochondria failed to restore phospholipid metabolism. These findings provide a novel mechanism in which the formation of functional protein complexes drives mitochondrial protein import. The EMBO Journal (2010) 29, 2875-2887. doi: 10.1038/emboj. 2010.149; Published online 9 July 2010
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