A 105-kDa protein is required for yeast mitochondrial RNase P activity.
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).
Morales
M J
MJ
Department of Biochemistry, University of Louisville, KY 40292.
Dang
Y L
YL
Lou
Y C
YC
Sulo
P
P
Martin
N C
NC
D000595:Amino Acid Sequence; D001483:Base Sequence; D004722:Endoribonucleases / Q000737:chemistry* / Q000302:isolation & purification; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification; D005800:Genes, Fungal; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016254:Mutagenesis, Insertional; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D016337:RNA, Catalytic / Q000737:chemistry* / Q000302:isolation & purification; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D009838:Oligodeoxyribonucleotides; D016337:RNA, Catalytic; D004722:Endoribonucleases; D043262:Ribonuclease P