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Vol. 14, Issue 6, 2303-2313, June 2003
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Institut für Physiologische Chemie, Universität München, D-81377 Munich, Germany
Submitted December 13, 2002;
Accepted January 30, 2003
Monitoring Editor: Thomas D. Fox
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 that is commonly found in subunits of Skp1-Cdc53-F-box
protein 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.
Corresponding author. E-mail address:
benedikt.westermann{at}bio.med.uni-muenchen.de.
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