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J. Cell Biol.,
Volume 145, Number 6, June 14, 1999 1199-1208
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.
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