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A more recent version of this article appeared on June 1, 2003
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Submitted on December 18, 2002
Accepted on January 30, 2003
1 Institut für Physiologische Chemie, Universität München, Butenandtstr. 5, D-81377 München Germany
* Corresponding author. E-mail address: benedikt.westermann{at}bio.med.uni-muenchen.de.
Mitochondrial fusion and fission play important roles for mitochondrial morphology and function. We identified Mdm30 as a novel component required for maintenance of fusion-competent mitochondria in yeast. The Mdm30 sequence contains an F-box motif which is commonly found in subunits of Skp1-Cdc53-F-box protein (SCF) ubiquitin ligases. A fraction of Mdm30 is associated with mitochondria. Cells lacking Mdm30 contain highly aggregated or fragmented mitochondria instead of the branched tubular network seen in wild type cells. 
mdm30 cells lose mitochondrial DNA at elevated temperature and fail to fuse mitochondria in zygotes at all temperatures. These defects are rescued by deletion of DNM1, a gene encoding a component of the mitochondrial division machinery. The protein level of Fzo1, a key component of the mitochondrial fusion machinery, is regulated by Mdm30. Elevated Fzo1 levels in cells lacking Mdm30 or in cells overexpressing Fzo1 from a heterologous promoter induce mitochondrial aggregation in a similar manner. Our results suggest that Mdm30 controls mitochondrial shape by regulating the steady state level of Fzo1 and point to a connection of the ubiquitin/26S proteasome system and mitochondria.
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