Abstract
RNase P in both prokaryotes and eukaryotes is a ribonucleoprotein that cleaves tRNA precursors to generate the 5′ termini of the mature tRNAs. Many patients with autoimmune diseases produce antibodies against a 40 kDa protein (designatedTo orTh antigen) which is an integral component of eukaryotic RNaseP as well as nucleolar 7-2 RNP which is identical to the mitochondrial RNA processing (MRP) RNP. Interestingly, theTo antigen found in human cells and the C5 protein, the only protein component ofE. coli RNaseP, are antigenically related. In this study, we show that a 56 nucleotide-long sequence, corresponding to nucleotides 20–75 near the 5′ end of human RNaseP RNA, is sufficient to bind theTo antigen. We previously showed that the humanTo antigen binds to a short distinct structural domain near the 5′ end of human 7-2/MRP RNA. There is no obvious primary sequence homology between theTo antigen binding sites in RNaseP RNA and 7-2/MRP RNA; however, these sequences are capable of assuming a similar secondary structure which corresponds to the recently proposed ‘cage’ structure for RNaseP RNAs and 7-2/MRP RNA (Forster and Altman (1989) Cell 62: 407–409). These data are supportive of the idea that these two RNAs may have evolved from a common progenitor molecule.
Similar content being viewed by others
References
Altman S, Gold H, Bartkiewcz M: Ribonuclease P as a snRNP. In: M Birnstiel (ed.) Structure and Function of Major and Minor snRNAs. Springer Verlag, 1988, pp 183–195
Baer M, Nilse TW, Costigan C, Altman S: Structure and transcription of a human gene for H1 RNA, the RNA component of human RNaseP. Nucl Acids Res 18: 97–103, 1990
Bartkewicz M, Gold H, Altman S: Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells. Genes Dev 3: 488–499, 1989
Brownlee GG, Sanger F, Barrell BG: The sequence of 5 S ribosomal ribonucleic acid. J Mol Biol 34: 379–412, 1968
Chang DD, Clayton DA: A novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replication. EMBO J 6: 409–417, 1987a
Chang DD, Clayton DA: A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA. Science 235: 1178–1184, 1987b
Chang DD, Clayton DA: Mouse RNase MRP RNA is encoded by a nuclear gene and contains a decamer sequence complementary to a conserved region of mitochondrial RNA substrate. Cell 56: 131–139, 1989
Das G, Henning D, Wright D, Reddy R: Upstream regulatory elements are necessary and sufficient for transcription of a U6 RNA gene by RNA polymerase III. EMBO J 7: 503–512, 1988
Dreyfuss G, Adams SA, Choi YD: Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. Mol Cell Biol 4: 415–423, 1984
Forster AC, Altman S: Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes. Cell 62: 407–409, 1990
Gold HA, Craft J, Hardin JA, Bartkiewicz M, Altman S: Antibodies in human serum that precipitate ribonuclease P. Proc Natl Acad Sci USA 85: 5483–5487, 1988
Gold HA, Topper JN, Clayton DA, Craft J: The RNA processing enzyme RNase MRP is identical to theTh RNP and related to RNase P. Science 245: 1377–1380, 1989
Greenberg JR: Proteins crosslinked to messenger RNA by irradiating polyribosomes with ultraviolet light. Nucl Acids Res 8: 5685–5701, 1980
Hashimoto C, Steitz JA: Sequential association of 7-2 RNA with two different autoantigens. J Biol Chem 258: 1379–1382, 1983
Kiss T, Filipowicz W: Evidence against a mitochondrial location of the 7-2/MRP RNA in mammalian cells. Cell 70: 11–15, 1992
Kiss T, Marshallsay C, Filipowicz W: 7-2/MRP RNAs in plant and mammalian cells: Association with higher order structures in the nucleolus. EMBO J 11: 3737–3746, 1992
Lerner M, Steitz JA: Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus. Proc Natl Acad Sci USA 76: 5495–5499, 1979
Mamula MJ, Baer M, Craft J, Altman S: An immunological determinant of RNase P protein is conserved betweenEscherichia coli and human. Proc Natl Acad Sci USA 86: 8717–8721, 1989
Reddy R, Li W, Henning D, Choi YC, Nohga K, Busch H: Characterization and subcellular localization of 7–8 S RNAs of Novikoff hepatoma cells. J Biol Chem 256: 8452–8457, 198
Reddy R, Tan EM, Henning D, Nohga K, Busch H: Detection of a nucleolar 7-2 ribonucleoprotein and a cytoplasmic 8-2 ribonucleoprotein with autoantibodies from patients with scleroderma. J Biol Chem 258: 1383–1386, 1983
Reimer G, Raska I, Scheer U, Tan EM: Immunolocalization of 7-2 ribonucleoprotein in the granular component of the nucleolus. Exp Cell Res 176: 117–128, 1988
Tan EM: Advances in immunology 44: 93–151, 1989
Topper JN, Clayton DA: Secondary structure of the RNA component of a nuclear mitochondrial ribonucleoprotein. J Biol Chem 265: 13254–13262, 1990
Vioque A, Arnez J, Altman S: Protein-RNA interactions in the RNase holenzyme fromEscherichia coli. J Mol Biol 202: 835–848, 1988
Weil PA, Segall J, Harris B, Ng S, Roeder R: J Biol Chem 234: 6163–6173, 1979
Yuan Y, Singh R, Reddy R: Rat nucleolar 7-2 RNA is homologous to mouse mitochondrial RNase mitochondrial RNA-processing RNA. J Biol Chem 264: 14835–14839, 1989
Yuan Y, Reddy R: 5′ flanking upstream sequences of MRP/7-2 RNA gene are required and sufficient for the transcription by RNA polymerase III. Biochem Biophys Acta 1089: 33–39, 1991
Yuan Y, Tan EM, Reddy R: A 40-kilodalton To autoantigen associates with nucleotides 21 to 64 of human mitochondrial RNA processing/7-2 RNAin vitro. Mol Cell Biol 11: 5266–5274, 1991
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Liu, MH., Yuan, Y. & Reddy, R. Human RNaseP RNA and nucleolar 7-2 RNA share conserved ‘To’ antigen-binding domains. Mol Cell Biochem 130, 75–82 (1994). https://doi.org/10.1007/BF01084270
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01084270