Abstract
Ribonuclease P cleaves 5'-precursor sequences from pre-tRNAs. All cellular RNase P holoenzymes contain homologous RNA elements; the eucaryal RNase P RNA, in contrast to the bacterial RNA, is catalytically inactive in the absence of the protein component(s). To understand the function of eucaryal RNase P RNA, knowledge of its structure is needed. Considerable effort has been devoted to comparative studies of the structure of this RNA from diverse organisms, including eucaryotes, primarily fungi, but also a limited set of vertebrates. The substantial differences in the sequences and structures of the vertebrate RNAs from those of other organisms have made it difficult to align the vertebrate sequences, thus limiting comparative studies. To expand our understanding of the structure of diverse RNase P RNAs, we have isolated by PCR and sequenced 13 partial RNase P RNA genes from 11 additional vertebrate taxa representing most extant major vertebrate lineages. Based on a recently proposed structure of the core elements of RNase P RNA, we aligned the sequences and propose a minimum consensus secondary structure for the vertebrate RNase P RNA.
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- Altman S., Kirsebom L., Talbot S. Recent studies of ribonuclease P. FASEB J. 1993 Jan;7(1):7–14. doi: 10.1096/fasebj.7.1.7916700. [DOI] [PubMed] [Google Scholar]
- Altman S., Wesolowski D., Puranam R. S. Nucleotide sequences of the RNA subunit of RNase P from several mammals. Genomics. 1993 Nov;18(2):418–422. doi: 10.1006/geno.1993.1488. [DOI] [PubMed] [Google Scholar]
- Baer M., Nilsen T. W., Costigan C., Altman S. Structure and transcription of a human gene for H1 RNA, the RNA component of human RNase P. Nucleic Acids Res. 1990 Jan 11;18(1):97–103. doi: 10.1093/nar/18.1.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Calvin N. M., Hanawalt P. C. High-efficiency transformation of bacterial cells by electroporation. J Bacteriol. 1988 Jun;170(6):2796–2801. doi: 10.1128/jb.170.6.2796-2801.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen J. L., Pace N. R. Identification of the universally conserved core of ribonuclease P RNA. RNA. 1997 Jun;3(6):557–560. [PMC free article] [PubMed] [Google Scholar]
- Doria M., Carrara G., Calandra P., Tocchini-Valentini G. P. An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes. Nucleic Acids Res. 1991 May 11;19(9):2315–2320. doi: 10.1093/nar/19.9.2315. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eder P. S., Srinivasan A., Fishman M. C., Altman S. The RNA subunit of ribonuclease P from the zebrafish, Danio rerio. J Biol Chem. 1996 Aug 30;271(35):21031–21036. doi: 10.1074/jbc.271.35.21031. [DOI] [PubMed] [Google Scholar]
- Fox G. E., Woese C. R. 5S RNA secondary structure. Nature. 1975 Aug 7;256(5517):505–507. doi: 10.1038/256505a0. [DOI] [PubMed] [Google Scholar]
- Guerrier-Takada C., Gardiner K., Marsh T., Pace N., Altman S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell. 1983 Dec;35(3 Pt 2):849–857. doi: 10.1016/0092-8674(83)90117-4. [DOI] [PubMed] [Google Scholar]
- Haas E. S., Armbruster D. W., Vucson B. M., Daniels C. J., Brown J. W. Comparative analysis of ribonuclease P RNA structure in Archaea. Nucleic Acids Res. 1996 Apr 1;24(7):1252–1259. doi: 10.1093/nar/24.7.1252. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haas E. S., Brown J. W., Pitulle C., Pace N. R. Further perspective on the catalytic core and secondary structure of ribonuclease P RNA. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2527–2531. doi: 10.1073/pnas.91.7.2527. [DOI] [PMC free article] [PubMed] [Google Scholar]
- James B. D., Olsen G. J., Pace N. R. Phylogenetic comparative analysis of RNA secondary structure. Methods Enzymol. 1989;180:227–239. doi: 10.1016/0076-6879(89)80104-1. [DOI] [PubMed] [Google Scholar]
- Kirsebom L. A., Svärd S. G. Base pairing between Escherichia coli RNase P RNA and its substrate. EMBO J. 1994 Oct 17;13(20):4870–4876. doi: 10.1002/j.1460-2075.1994.tb06814.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Li K., Williams R. S. Cloning and characterization of three new murine genes encoding short homologues of RNase P RNA. J Biol Chem. 1995 Oct 20;270(42):25281–25285. doi: 10.1074/jbc.270.42.25281. [DOI] [PubMed] [Google Scholar]
- Maidak B. L., Larsen N., McCaughey M. J., Overbeek R., Olsen G. J., Fogel K., Blandy J., Woese C. R. The Ribosomal Database Project. Nucleic Acids Res. 1994 Sep;22(17):3485–3487. doi: 10.1093/nar/22.17.3485. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oh B. K., Pace N. R. Interaction of the 3'-end of tRNA with ribonuclease P RNA. Nucleic Acids Res. 1994 Oct 11;22(20):4087–4094. doi: 10.1093/nar/22.20.4087. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sbisà E., Pesole G., Tullo A., Saccone C. The evolution of the RNase P- and RNase MRP-associated RNAs: phylogenetic analysis and nucleotide substitution rate. J Mol Evol. 1996 Jul;43(1):46–57. doi: 10.1007/BF02352299. [DOI] [PubMed] [Google Scholar]
- Vioque A. The RNase P RNA from cyanobacteria: short tandemly repeated repetitive (STRR) sequences are present within the RNase P RNA gene in heterocyst-forming cyanobacteria. Nucleic Acids Res. 1997 Sep 1;25(17):3471–3477. doi: 10.1093/nar/25.17.3471. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zuker M. On finding all suboptimal foldings of an RNA molecule. Science. 1989 Apr 7;244(4900):48–52. doi: 10.1126/science.2468181. [DOI] [PubMed] [Google Scholar]