Comparative structural analysis of nuclear RNase P RNAs from yeast

Tranguch, Anthony J.; Engelke, David R.

doi:10.1016/s0021-9258(19)85207-9

Cited by 62 publications

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“…1). The eukaryotic P3 region is composed of a helixloop-helix structure as opposed to the continuous stem structure in the bacterial P3 (Schmitt et al, 1993;Tranguch and Engelke, 1993;Paluh and Clayton, 1995;Pitulle et al, 1998;Schmitt, 1999). The variation in structure is consistent with the possible functions of P3 in eukaryotes.…”

Section: The Rna Subunitsupporting

confidence: 52%

Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

2001

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Ribonuclease P is an ancient enzyme that cleaves pre-tRNAs to generate mature 5' ends. It contains an essential RNA subunit in Bacteria, Archaea, and Eukarya, but the degree to which the RNA subunit relies on proteins to supplement catalysis is highly variable. The eukaryotic nuclear holoenzyme has recently been found to contain almost twenty times the protein content of the bacterial enzymes, in addition to having split into at least two related enzymes with distinct substrate specificity. In this review, recent progress in understanding the molecular architecture and functions of nuclear forms of RNase P will be considered.

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Section: The Rna Subunitsupporting

confidence: 52%

Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

2001

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“…Five primers were used in this study to span the entire length of the RNase P RNA. Positions to which these primers hybridized are shown in Figure 1 relative to the secondary structure model, previously proposed on the basis of phylogenetic analysis of yeast nuclear RNase P RNAs (Tranguch & Engelke, 1993). Refinements to this structure, based on results from the current study, are shown as shaded areas in this figure and are incorporated into the structure models displayed in subsequent figures.…”

Section: Resultsmentioning

confidence: 99%

“…Immediately following addition of the chemical reagent, samples were mixed gently by pipetting. Reactions were terminated by the addition of 200 pL of stop buffer (buffer H for DMS and CMCT, Figure 1: Previous secondary structure model for S. cerevisiae nuclear RNase P RNA based on comparative sequence analysis (Tranguch & Engelke, 1993). Nucleotides found to be invariant among the Saccharomyces nuclear RNAs are circled.…”

Section: Methodsmentioning

confidence: 99%

“…Difficulties in deriving an unequivocal structure for the mitochondrial RNA subunits involve their extremely high (>85%) A+U sequence content (Morales et al, 1989). The structures of the nuclear RNase P RNAs have recently been shown to contain some regions of structural homology to the eubacterial RNAs (Forster & Altman, 1990;Tranguch & Engelke, 1993). Whereas the protein subunit comprises only a small percentage of the eubacterial RNase P, protein accounts for ~50% (by density) of the eukaryotic holoenzymes (Kline et al, 1981;Lawrence et al, 1987;Morales et al, 1989;Doria et al, 1991;Jayanthi & Van Tuyle, 1992) and at least one of the archaebacterial holoenzymes (Darr et al, 2 S. J. Talbot and S. Altman, personal communication. 0006-2960/94/0433-1778$04.50/0 © 1994 American Chemical Society 1990).…”

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confidence: 99%

“…Our laboratory had previously identified the RNA component of S. cerevisiae nuclear RNase P (Lee & Engelke, 1989), characterized its gene (RPR1), and demonstrated through defective alleles that it was an essential component of nuclear RNase P (Lee et al, 1991). We subsequently characterized the RNase P RNAs and their genes from six Saccharomyces species and derived secondary structure models for the RNAs via comparative sequence analysis (Tranguch & Engelke, 1993). A common core of primary and secondary structure emerged for the Saccharomyces RNase P RNAs, and the Schizosaccharomyces homologs conformed in large part to this consensus structure.…”

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confidence: 99%

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Structure-Sensitive RNA Footprinting of Yeast Nuclear Ribonuclease P

et al. 1994

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Several enzymatic and chemical reagents were used to probe the secondary structure of Saccharomyces cerevisiae nuclear RNase P RNA in the presence and absence of its protein components. Double-stranded regions were detected with RNase V1 and single-stranded regions with RNase ONE (Escherichia coli RNase I). Nucleotides not paired at Watson-Crick positions were monitored with dimethyl sulfate, kethoxal, and 1-cyclohexyl-3-[2-(N-methylmorpholinio)ethyl]carbodiimide p-toluenesulfonate. The results supported most aspects of the previously proposed, phylogenetically-derived RNA secondary structure, although minor refinements allowed incorporation of both the biochemical and phylogenetic data. Digestion of the RNase P protein(s) with proteinase K gave enhanced reactivities to structure probes at selected positions, indicating regions of the RNA made inaccessible by the presence of the protein subunit(s). The regions of RNA protected in the yeast nuclear holoenzyme were considerably more extensive than that seen in the Escherichia coli holoenzyme, consistent with the observation that the protein moiety generally comprises a larger percentage of the RNase P holoenzyme in eukaryotes than in eubacteria.

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RibonucleaseP

Florentz

Martín

2002

Encyclopedia of Molecular Biology

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Comparative structural analysis of nuclear RNase P RNAs from yeast

Cited by 62 publications

References 0 publications

Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

Structure-Sensitive RNA Footprinting of Yeast Nuclear Ribonuclease P

RibonucleaseP

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