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A more recent version of this article appeared on April 1, 2004
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Submitted on June 6, 2003
Revised on December 19, 2003
Accepted on January 14, 2004
1 University of California, San Diego, Division of Biological Sciences, Section of Cell and Developmental Biology, La Jolla, California 92093
* Corresponding author. E-mail address: myaffe{at}ucsd.edu.
The mmd1 mutation causes temperature-sensitive growth and defects in mitochondrial morphology and distribution in the fission yeast, Schizosaccharomyces pombe. In mutant cells, mitochondria aggregate at the two cell ends, with increased aggregation at elevated temperatures. Microtubules, which mediate mitochondrial positioning in fission yeast, appear normal in mmd1 cells at permissive temperature and after several hours at the nonpermissive temperature but display aberrant organization after prolonged periods at 37°C. Additionally, cells harboring both mmd1 and ban5-4, a temperature-sensitive allele of 
2-tubulin, display synthetic defects in growth and mitochondrial distribution. The mmd1 mutation maps to an open reading frame encoding a novel 35.7 kDa protein. The Mmd1p sequence features repeating EZ-HEAT motifs and displays high conservation with uncharacterized homologues found in a variety of organisms. S. cerevisiae cells depleted for their MMD1 homolog show increased sensitivity to the antimicrotubule drug benomyl, and the S. cerevisiae gene complemented the S. pombe mutation. Mmd1p was localized to the cytosol. Mmd1p is the first identified component required for the alignment of mitochondria along microtubules in fission yeast.
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