A 105-kDa protein is required for yeast mitochondrial RNase P activity.

Morales, Michael J.; Dang, Yan L.; Lou, Yan; Sulo, Pavol; Martín, Nancy

doi:10.1073/pnas.89.20.9875

Cited by 83 publications

(55 citation statements)

References 47 publications

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“…It is likely compensated by increase in size and/or number of P-proteins (e.g., the large size of the mitochondrial P-protein in S. cerevisiae; Morales et al 1992;Dang and Martin 1993) and the possibility of multiple mitochondrial P-proteins in A. nidulans (Lee et al 1996b). An investigation of fungal mitochondrial P-proteins and of native mtP-RNA enzymes could be useful in shedding light on the principles related to the replacement of RNA by protein structure.…”

Section: Mitochondrial Rnase P Rnas In Ascomycete Fungimentioning

confidence: 99%

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Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure

Seif¹,

Forget²,

Martín³

et al. 2003

RNA

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The RNA subunit of mitochondrial RNase P (mtP-RNA) is encoded by a mitochondrial gene (rnpB) in several ascomycete fungi and in the protists Reclinomonas americana and Nephroselmis olivacea. By searching for universally conserved structural elements, we have identified previously unknown rnpB genes in the mitochondrial DNAs (mtDNAs) of two fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces octosporus; in the budding yeast Pichia canadensis; and in the archiascomycete Taphrina deformans. The expression of mtP-RNAs of the predicted size was experimentally confirmed in the two fission yeasts, and their precise 5 and 3 ends were determined by sequencing of cDNAs generated from circularized mtP-RNAs. Comparative RNA secondary structure modeling shows that in contrast to mtP-RNAs of the two protists R. americana and N. olivacea, those of ascomycete fungi all have highly reduced secondary structures. In certain budding yeasts, such as Saccharomycopsis fibuligera, we find only the two most conserved pairings, P1 and P4. A P18 pairing is conserved in Saccharomyces cerevisiae and its close relatives, whereas nearly half of the minimum bacterial consensus structure is retained in the RNAs of fission yeasts, Aspergillus nidulans and Taphrina deformans. The evolutionary implications of the reduction of mtP-RNA structures in ascomycetes will be discussed.

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Section: Mitochondrial Rnase P Rnas In Ascomycete Fungimentioning

confidence: 99%

“…Its RNA subunit was first identified as a mitochondrially encoded molecule by analyzing yeast mitochondrial mutants deficient in mitochondrial tRNA processing and protein synthesis Underbrink-Lyon et al 1983). The unusually large protein subunit has been shown to be nucleus-encoded (Morales et al 1992;Dang and Martin 1993).…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure

Seif¹,

Forget²,

Martín³

et al. 2003

RNA

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“…The similarity between this estimate and the size of POPlp (100.5 kD)suggests that this S. pombe protein is the homolog of POPlp. A protein component of the S. cerevisiae mitochondrial RNase P, encoded by the RPM2 gene, has also been characterized (Morales et al 1992;Dang and Martin 1993). This protein has a molecular mass of 105 kD and is essential for mitochondrial RNase P function in vivo but has no significant homology to POPlp.…”

Section: Pop1 Is a Component Of Rnase P And Rnase Mrpmentioning

confidence: 99%

The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins.

Lygerou¹,

Mitchell²,

Petfalski³

et al. 1994

Genes Dev.

198

214

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Two forms of the yeast 5.8S rRNA are generated from a large precursor by distinct processing pathways. Cleavage at site A3 is required for synthesis of the major, short form, designated 5.8S(S), but not for synthesis of the long form, 5.8S(L). To identify components required for A3 cleavage, a bank of temperature-sensitive lethal mutants was screened for those with a reduced ratio of 5.8S(S):5.8S(L). The pop1-1 mutation (for processing of precursor RNAs) shows this phenotype and also inhibits A3 cleavage. The pre-rRNA processing defect of pop1-1 strains is similar to that reported for mutations in the RNA component of RNase MRP; we show that a mutation in the RNase MRP RNA also inhibits cleavage at site A3. This is the first site shown to require RNase MRP for cleavage in vivo. The pop1-1 mutation also leads to a block in the processing of pre-tRNA that is identical to that reported for mutations in the RNA component of RNase P. The RNA components of both RNase MRP and RNase P are underaccumulated in pop1-1 strains at the nonpermissive temperature, and immunoprecipitation demonstrates that POPlp is a component of both ribonucleoproteins.The POP1 gene encodes a protein with a predicted molecular mass of 100.5 kD and is essential for viability.POPlp is the first protein component of the nuclear RNase P or RNase MRP for which the gene has been cloned.[Key Words: POP1 gene; RNase MRP; RNase P; S. cerevisiae; RNA processing] Received April 4, 1994; revised version accepted May 9, 1994.Two ribonucleoprotein (RNP) complexes are known to have endoribonuclease (RNase) activity. These are the RNase P and RNase mitochondrial RNA processing (MRP) RNPs.All pre-tRNAs are transcribed with 5' and 3' extensions, and some contain intervening sequences that are removed to produce the mature tRNAs. RNase P is responsible for the 5' processing of pre-tRNAs in eubacteria, archaebacteria, and eukaryotes (for review, see Altman 1989;Dart et al. 1992;Altman et al. 1993). RNase P also processes the precursor of the 4.5S RNA in Escherichia coli (for review, see by Altman et al. 1993) but has not been reported to have substrates other than pretRNAs in archaebacteria or eukaryotes. The RNA component of eubacterial RNase P has catalytic activity in vitro in the absence of protein cofactors. In contrast, the RNA components of archaebacterial (Nieuwlandt et al. 1991;LaGrandeur et al. 1993) and eukaryotic RNase P have not been found to be catalytic in the absence of proteins, despite their considerable structural homology to the eubacterial RNAs. E. coli RNase P contains a single protein, designated C5, which is small (119 amino acids, 13.8 kD) and highly basic. This protein cofactor is required for RNase P activity in vivo and greatly stimulates activity in vitro. The protein plays important roles in the release of the product, the mature tRNA, from the enzyme, which is the rate-limiting step for the RNA catalyzed reaction in vitro (Reich et al. 1988;Tallsj6 and Kirsebom 1993), and in the binding of suboptimal substrates, including the 4.5S RN...

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“…Purification of mitochondrial RNase P to near homogeneity revealed a protein of -105 kDa fractionating with enzyme activity (6). The gene coding for this protein was isolated and a genetic approach was used to determine if it played a role in RNase P activity.…”

Section: Introductionmentioning

confidence: 99%

Successful transformation of yeast mitochondria withRPM1: an approach forin vivostudies of mitochondrial RNase P RNA structure, function and biosynthesis

et al. 1995

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Mitochondrial RNase P RNA (Rpmlr) is coded by the RPM1 gene of mitochondrial DNA in many yeasts. As an initial step to developing a genetic approach to the structure and biogenesis of yeast mitochondrial RNase P, biolistic transformation has been used to introduce wild type and altered RPM1 genes into strains containing no mitochondrial DNA. The introduced wild type gene does support RNase P activity demonstrating that pre existing RNase P activity is not necessary for the biosynthesis of the enzyme. Mutations introduced into RPM1 in vitro result in reduced accumulation of mature tRNA and in an alteration of the processing of Rpml r in vivo.

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A 105-kDa protein is required for yeast mitochondrial RNase P activity.

Cited by 83 publications

References 47 publications

Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure

Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure

The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins.

Successful transformation of yeast mitochondria withRPM1: an approach forin vivostudies of mitochondrial RNase P RNA structure, function and biosynthesis

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