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© The Rockefeller University Press, 0021-9525/1999//1199 $5.00
The Journal of Cell Biology, Volume 145, Number 6, , 1999 1199-1208

A Role for Ubiquitination in Mitochondrial Inheritance in Saccharomyces cerevisiae

University of California, San Diego, Department of Biology, La Jolla, California 92093

The smm1 mutation suppresses defects in mitochondrial distribution and morphology caused by the mdm1-252 mutation in the yeast Saccharomyces cerevisiae. Cells harboring only the smm1 mutation themselves display temperature-sensitive growth and aberrant mitochondrial inheritance and morphology at the nonpermissive temperature. smm1 maps to RSP5, a gene encoding an essential ubiquitin-protein ligase. The smm1 defects are suppressed by overexpression of wild-type ubiquitin but not by overexpression of mutant ubiquitin in which lysine-63 is replaced by arginine. Furthermore, overexpression of this mutant ubiquitin perturbs mitochondrial distribution and morphology in wild-type cells. Site-directed mutagenesis revealed that the ubiquitin ligase activity of Rsp5p is essential for its function in mitochondrial inheritance. A second mutation, smm2, which also suppressed mdm1-252 defects, but did not cause aberrant mitochondrial distribution and morphology, mapped to BUL1, encoding a protein interacting with Rsp5p. These results indicate that protein ubiquitination mediated by Rsp5p plays an essential role in mitochondrial inheritance, and reveal a novel function for protein ubiquitination.

Key Words: mitochondria • ubiquitin • yeast • organelle inheritance • cytoskeleton

Abbreviations used in this paper: CIP, calf intestinal phosphatase; DAPI, 4,6-diamidino-2-phenylindole; DASPMI, 2-(4-dimethylaminostyryl)-1-methylpyridinium iodide; YPD, yeast extract/peptone/glucose.

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