Proceedings of the National Academy of Sciences · 1992 · 90 citations · 49 references
Life SciencesBiochemistryMolecular BiologyEnzymologyMitochondrial BiologyMitochondrial GeneticsMitochondrial BiochemistryMitochondrial FunctionMitochondrial Rna ProcessingMitochondrial 5' End ProcessingMitochondrial Messenger RnasMitochondrial Rnase PMitochondrial Transfer Rna GenesMitochondrial Trna ProcessingYeast Mitochondrial BiologyYeast Mitochondrial Genetics
RNase P from the mitochondria of Saccharomyces cerevisiae was purified to near homogeneity > 1800-fold with a yield of 1.6% from mitochondrial extracts. The most abundant protein in the purified fractions is, at 105 kDa, considerably larger than the 14-kDa bacterial RNase P protein subunits. Oligonucleotides designed from the amino-terminal sequence of the 105-kDa protein were used to identify and isolate the 105-kDa protein-encoding gene. Strains carrying a disruption of the gene for the 105-kDa protein are viable but respiratory deficient and accumulate mitochondrial tRNA precursors with 5' extensions. As this is the second gene known to be necessary for yeast mitochondrial RNase P activity, we have named it RPM2 (for RNase P mitochondrial).
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Measurement of protein using bicinchoninic acid
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The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
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