Abstract
Previous studies on certain altered holo-isocytochromes c revealed a ρ--dependent degradation (RDD) phenotype, in which certain altered holo-iso-1-cytochromes c are at normal or nearly normal levels in ρ+ strains, but are at low levels or absent in ρ- strains, although wild-type holo-iso-1-cytochrome c is present at normal levels in both ρ+ and related ρ- strains. The diminished levels of altered holo-iso-1-cytochrome c are due to the rapid degradation that is carried out by a novel proteolytic pathway in the IMS of mitochondria. SUE1, a nuclear gene that encodes a mitochondrial protein, was identified with a genetic screen for mutants that diminish RDD. The levels of RDD and certain other types of altered holo-iso-1-cytochrome c were elevated in ρ- sue1 strains. Also, ρ+ sue1 strains containing certain altered holo-iso-1-cytochromes c grew better on non-fermentable carbon sources than the corresponding ρ+ SUE1 strains. These results indicate that Sue1p may play an important role in the degradation of abnormal holo-iso-1-cytochrome c in the mitochondria.
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CITATION STYLE
Wei, J., & Sherman, F. (2004). Sue1p is required for degradation of labile forms of altered cytochromes c in yeast mitochondria. Journal of Biological Chemistry, 279(29), 30449–30458. https://doi.org/10.1074/jbc.M403742200
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