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Published 18 February 2003. doi:10.1083/jcb.200211113
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© The Rockefeller University Press, 0021-9525/2003/2/553 $5.00
The Journal of Cell Biology, Volume 160, Number 4, 553-564

Article

The inner membrane protein Mdm33 controls mitochondrial morphology in yeast



Marlies Messerschmitt1, Stefan Jakobs2, Frank Vogel3, Stefan Fritz1, Kai Stefan Dimmer1, Walter Neupert1 and Benedikt Westermann1

1 Institut für Physiologische Chemie, Universität München, D-81377 München, Germany
2 High Resolution Optical Microscopy Group, Max-Planck-Institut für Biophysikalische Chemie, D-37077 Göttingen, Germany
3 Electron Microscopy Group, Max-Delbrück-Centrum für Molekulare Medizin, D-13092 Berlin, Germany

Address correspondence to Benedikt Westermann, Institut für Physiologische Chemie, Universität München, Butenandtstr. 5, D-81377 München, Germany. Tel.: 49-89-2180-77122. Fax: 49-89-2180-77093. E-mail: benedikt.westermann{at}bio.med.uni-muenchen.de

Mitochondrial distribution and morphology depend on MDM33, a Saccharomyces cerevisiae gene encoding a novel protein of the mitochondrial inner membrane. Cells lacking Mdm33 contain ring-shaped, mostly interconnected mitochondria, which are able to form large hollow spheres. On the ultrastructural level, these aberrant organelles display extremely elongated stretches of outer and inner membranes enclosing a very narrow matrix space. Dilated parts of {Delta}mdm33 mitochondria contain well-developed cristae. Overexpression of Mdm33 leads to growth arrest, aggregation of mitochondria, and generation of aberrant inner membrane structures, including septa, inner membrane fragments, and loss of inner membrane cristae. The MDM33 gene is required for the formation of net-like mitochondria in mutants lacking components of the outer membrane fission machinery, and mitochondrial fusion is required for the formation of extended ring-like mitochondria in cells lacking the MDM33 gene. The Mdm33 protein assembles into an oligomeric complex in the inner membrane where it performs homotypic protein–protein interactions. Our results indicate that Mdm33 plays a distinct role in the mitochondrial inner membrane to control mitochondrial morphology. We propose that Mdm33 is involved in fission of the mitochondrial inner membrane.

Key Words: membrane fission; mitochondria; mitochondrial dynamics; organelle morphology; Saccharomyces cerevisiae


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