The RNA component of RNase P in <i>Schizosaccharomyces</i> species

Zimmerly, Steven; Gamulin, Vera; Burkard, Ulrike; Söll, Dieter

doi:10.1016/0014-5793(90)80403-6

Cited by 20 publications

(12 citation statements)

References 22 publications

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“…RNase P has also been purified from a few members of the Eucarya, specifically fungi (12,13,23) and vertebrates (3,8); however, little is known about the structure of those enzymes. The eucaryal RNase P activities copurify with RNAs that have been isolated and sequenced, but the RNAs are not catalytically active in the absence of protein components.…”

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confidence: 99%

Characterization of the RNase P RNA of Sulfolobus acidocaldarius

et al. 1993

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RNase P is the ribonucleoprotein enzyme that cleaves precursor sequences from the 5' ends of pre-tRNAs. In Bacteria, the RNA subunit is the catalytic moiety. Eucaryal and archaeal RNase P activities copurify with RNAs, which have not been shown to be catalytic. We report here the analysis of the RNase P RNA from the thermoacidophilic archaeon Sudfolobus ocanarius. The holoenzyme was highly purified, and extracted RNA was used to identify the RNase P RNA gene. The nucleotide sequence of the gene was determined, and a secondary structure is proposed. The RNA was not observed to be catalytic by itself, but it nevertheless is similar in sequence and structure to bacterial RNase P RNA. The marked similarity of the RNase P RNA from S. acidocaldarius and that from Haloferax vokcanii, the other known archaeal RNase P RNA, supports the coherence of Archaea as a phylogenetic domain.RNase P is the ubiquitous endonuclease that cleaves leader sequences from precursors of tRNA to generate their mature 5' ends (1, 6, 15 previously known as eubacteria, "Archaea" refers to the phylogenetic group previously called archaebacteria, and "Eucarya" refers to organisms of the eucaryotic nuclear lineage.) The RNA moiety of the bacterial RNase P is the catalytic subunit: in vitro, at high ionic strength, the RNA can perform cleavage in the absence of the protein (9). A phylogenetic comparative analysis of RNase P RNA sequences has been used to infer secondary structures for bacterial RNAs, among which a conserved minimum of sequence and secondary structure is identifiable (4).RNase P has also been purified from a few members of the Eucarya, specifically fungi (12, 13, 23) and vertebrates (3, 8); however, little is known about the structure of those enzymes. The eucaryal RNase P activities copurify with RNAs that have been isolated and sequenced, but the RNAs are not catalytically active in the absence of protein components. The fungal and vertebrate-type RNAs possess little sequence similarity to one another or to bacterial RNase P RNAs, and they seem to lack structural elements present in the bacterial RNAs. The eucaryal RNase P's inspected appear to have a much higher content of protein than do their bacterial counterparts. This conclusion is based on the masses of the holoenzymes relative to the sizes of the putative RNA elements and the low buoyant densities of the holoenzymes in Cs2SO4 gradients, nearly that of protein alone.The RNase P from the third primary evolutionary lineage, * Corresponding author. the Archaea, offers further perspective on the fundamental properties of RNase P. RNase P from two phylogenetically diverse members of the Archaea, the halophile Haloferax volcanji (14) and the thermoacidophile Sulfolobus acidocaldarius (7), has been examined. An RNA from the H. volcanii enzyme has been described previously (14). Despite having a secondary structure that appears highly similar to that of bacterial RNase P RNA, this RNA was not catalytic without protein. The RNase P from S. acidocaldarius has intriguing properties si...

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confidence: 99%

Characterization of the RNase P RNA of Sulfolobus acidocaldarius

et al. 1993

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“…The data base for eukaryotic RNase P RNAs that function to process nuclear-coded tRNAs is small compared with that of prokaryotes. RNase P RNA genes that remove 5' leaders from nuclear-coded tRNAs in human (8), Xenopus (9), Schizosaccharomyces pombe (23), and Saccharomyces cerevisiae (6) have been sequenced. Although there have been models of eukaryotic RNase P RNAs proposed (6,8,23,24), extensive phylogenetic comparisons are not yet possible.…”

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confidence: 99%

“…RNase P RNA genes that remove 5' leaders from nuclear-coded tRNAs in human (8), Xenopus (9), Schizosaccharomyces pombe (23), and Saccharomyces cerevisiae (6) have been sequenced. Although there have been models of eukaryotic RNase P RNAs proposed (6,8,23,24), extensive phylogenetic comparisons are not yet possible. RNase P RNAs required for mitochondrial RNase P activity in yeast are coded by mitochondrial DNA (25), they are extremely A+U rich (26)(27)(28), and they vary in size from 140 to >490 nucleotides in different strains (29).…”

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confidence: 99%

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

Morales

Dang

Lou

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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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).RNase P removes 5' leaders from tRNA precursors and is an RNA-protein complex in bacteria (1-3), yeasts (4-6), and metazoans (7-9). The bacterial enzymes are the best characterized and consist of RNAs around 300 nucleotides and proteins in the 14-kDa size range (10). Genes for bacterial RNase P protein subunits from Escherichia coli (11), Bacillus subtilis (12), Proteus mirabilis (13), Micrococcus luteus (14), and Streptomyces bikiniesis (15) have been isolated and sequenced. They are all -14 kDa in size and have an abundance of charged amino acids. The buoyant densities of the E. coli enzyme at 1.55 g/cm3 (16) and the Haloferax volcanii enzyme at 1.61 g/cm3 (17) reflect their RNA-protein composition. In contrast, the RNase P from Sulfolobus solfataricus (18) appears more proteinaceous, with a buoyant density of 1.28 g/cm3. Even though the primary structures of RNAs and proteins are known for some bacterial enzymes, neither the structure of the holoenzyme nor the function of the protein in bacteria is understood.Although both the protein and RNA subunits of the bacterial enzymes are essential in vivo, in vitro the RNAs are catalytic (19). Comparisons of prokaryotic RNase P RNA genes (20,21) have produced a secondary structural model that has been further refined by genetic analyses (22). The data base for eukaryotic RNase P RNAs that function to process nuclear-coded tRNAs is small compared with that of prokaryotes. RNase P RNA genes that remove 5' leaders from nuclear-coded tRNAs in human (8), Xenopus (9), Schizosaccharomyces pombe (23), and Saccharomyces cerevisiae (6) have been sequenced. Although there have been models of eukaryotic RNase P RNAs proposed (6,8,23,24), extensive phylogenetic comparisons are not yet possible. RNase P RNAs required for mitochondrial RNase P activity in yeast are coded by mitochondrial DNA (25), they are extremely A+U rich (26-28), and they vary in size from 140 to >490 nucleotides in different strains (29). Despite their A+U-rich nature, all contain two short blocks of sequence similarity found in other RNase P RNAs, suggesting the functional importance of these short regions (27)(28)(29). No eukaryotic RNase P RNAs have been shown to be catalytic in the absence of protein but other than that they are ribonucleoprotein complexes, no...

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“…It is a single-copy gene which is transcribed by RNA polymerase III in vivo starting from canonical promoters but located in the leader region upstream of the mature RNA structural domain (Tranguch and Engelke 1993). In Schizosaccharomycetes the nuclear RNase P copurifies with two RNA species (K1 and K2) differing only in length (285-270) and transcribed by the same single-copy gene (Zimmerly et al 1990). The most recent hypothesis predicts that only one RNA, rather than one molecule of each RNA, is present per holoenzyme.…”

Section: Yeast Nuclear Rnase P Rnasmentioning

confidence: 99%

“…Indeed, the RNA components of both can be folded into a similar secondary structure (Forster and Altman 1990) (Yuan et al 1989) (Chang and Clayton 1989) (Bennett et al 1992) (Kiss et al 1992) (Schmitt and Ctayton 1992) (Bartkiewicz et al 1989) (Harmon et al 1991) (Baer et al 1990) (Altman et al 1993b) (Altman et al 1993b) (Altman et al 1993b) (Altman et al 1993b) (Altman et al 1993b) (Altman et al 1993b) (Altman et al 1993b) (Doria et aI. 1991 (Krupp et al 1986) (Zimmerly et al 1990) (Zimmerly et al 1990) (Zimmerly et al 1990) (Zimmerly et al 1990) (Zimmerly et al 1990) 1993) 1993) 1993) 1993) 1993) 1993) (Miller and Martin 1983) (Ragnini et al 1991) (Shu et al 1991…”

Section: Introductionmentioning

confidence: 96%

The evolution of the RNase P- and RNase MRP-associated RNAs: Phylogenetic analysis and nucleotide substitution rate

et al. 1996

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We report a detailed evolutionary study of the RNase P- and RNase MRP- associated RNAs. The analyses were performed on all the available complete sequences of RNase MRP (vertebrates, yeast, plant), nuclear RNase P (vertebrates, yeast), and mitochondrial RNase P (yeast) RNAs. For the first time the phylogenetic distance between these sequences and the nucleotide substitution rates have been quantitatively measured.The analyses were performed by considering the optimal multiple alignments obtained mostly by maximizing similarity between primary sequences. RNase P RNA and MRP RNA display evolutionary dynamics following the molecular clock. Both have similar rates and evolve about one order of magnitude faster than the corresponding small rRNA sequences which have been, so far, the most common gene markers used for phylogeny. However, small rRNAs evolve too slowly to solve close phylogenetic relationships such as those between mammals. The quicker rate of RNase P and MRP RNA allowed us to assess phylogenetic relationships between mammals and other vertebrate species and yeast strains. The phylogenetic data obtained with yeasts perfectly agree with those obtained by functional assays, thus demonstrating the potential offered by this approach for laboratory experiments.

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The RNA component of RNase P in Schizosaccharomyces species

Abstract: In the fission yeast Schixwarcharomyces pombe, the enzyme RNAse P copurifies with two RNAs, Kl-and KZ-RNA, which are identical except for their termini [I]

Cited by 20 publications

References 22 publications

Characterization of the RNase P RNA of Sulfolobus acidocaldarius

Characterization of the RNase P RNA of Sulfolobus acidocaldarius

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

The evolution of the RNase P- and RNase MRP-associated RNAs: Phylogenetic analysis and nucleotide substitution rate

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