Abstract
Ribosomes, ribosomal proteins (r-proteins), and messenger and transfer RNAs catalyze the synthesis of proteins in organisms. To understand and define the components involved in this event in Taenia solium, we isolated and characterized a T. solium cDNA encoding the basic ribosomal protein S15a (TsS15a). The TsS15a cDNA produces a protein with M r (relative molecular mass) 14,988, which contains 22.3% of basic amino acids. Analysis comparing TsS15a protein with other S15a r-proteins indicates that this protein is highly conserved. A recombinant TsS15a protein with similar M r was produced in bacteria. Antibodies against recombinant TsS15a react with a 15-kDa protein in extracts from all life stages of T. solium and from all helminths tested. Hybridization studies showed the presence of two genes encoding a mRNA of 0.5 kb. Moreover, the gene presents an intron of 30 bp. Our phylogenetic analysis using S15a r-proteins reproduced the topologies reported for 16/18S rRNA.
Similar content being viewed by others
References
Angerer LM, Yang Q, Liesveld J, Kingsley PD, Angerer RC (1992) Tissue-restricted accumulation of a ribosomal protein mRNA is not coordinated with rRNA transcription and precedes growth of the sea urchin pluteus larva. Dev Biol 149:27–40
Bergkamp-Steffens GK, Hoekstra R, Planta RJ (1992) Structural and putative regulatory sequences of Kluyveromyces ribosomal protein genes. Yeast 8:903–922
Bonham-Smith PC, Moloney MM (1994) Nucleotide and protein sequences of a cytoplasmic ribosomal protein S15a gene from Arabidopsis thaliana. Plant Physiol 106:401–402
Bonham-Smith PC, Oancia TL, Moloney MM (1992) Cytoplasmic ribosomal protein S15a from Brassica napus : molecular cloning and developmental expression in mitotically active tissues. Plant Mol Biol 18:909–919
Breathnach R, Chambon P (1981) Organization and expression of eukaryotic split genes coding for proteins. Annu Rev Biochem 50:349–383
Chan YL, Olvera J, Paz V, Wool IG (1994) The primary structure of rat ribosomal protein S15a. Biochem Biophys Res Commun 200:1498–1504
Dos Reis MG, Davis RE, Singh H, Skelly PJ, Shoemaker CB (1993) Characterization of the Schistosoma mansoni gene encoding the glycolytic enzyme, triosephosphate isomerase. Mol Biochem Parasitol 59:235–242
Gingras AC, Raught B, Sonenberg N (1999) eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 68:913–963
Hershey JWB, Merrick WC (2000) Pathway and mechanism of initiation of protein synthesis. In: Hershey JWB et al. (eds) Translational regulation of gene expression. Cold Spring Harbor Laboratory Press, pp 33–88
Jiménez L, Vibanco-Pérez N, Navarro L, Landa A (2000) Cloning, expression and characterisation of a recombinant triosephosphate isomerase from Taenia solium. Int J Parasitol 30:1007–1012
Kalinna BH, McManus DP (1996) Cloning and characterization of a ribosomal P protein from Taenia solium, the aetiological agent of human cysticercosis. Biochem Biophys Res Commun 219:231–237
Lavoie C, Tam R, Clark M, Lee H, Sonenberg N, Lasko P (1994) Suppression of a temperature-sensitive cdc33 mutation of yeast by a multicopy plasmid expressing a Drosophila ribosomal protein. J Biol Chem 269:14625–14630
Leer RJ, Van Raamsdonk-Duin MM, Kraakman P, Mager WH, Planta RJ (1985) The genes for yeast ribosomal proteins S24 and L26 are adjacent and divergently transcribed. Nucleic Acids Res 13:701–709
Matte-Tailliez O, Brochier C, Forterre P, Philippe H (2002) Archaeal phylogeny based on the ribosomal proteins. Mol Biol Evol 19:631–639
Padgett RA, Grabowski PJ, Konarska MM, Seiler S, Sharp PA (1986) Splicing of messenger RNA precursors. Annu Rev Biochem 55:1119–1150
Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
Sgroi A, Colombo P, Duro G, Fried M, Izzo V, Giudice G (1996) cDNA sequence analysis and expression of the expression of the ribosomal protein S24 during oogenesis and embryonic development of the sea urchin Paracentratus lividus. Biochem Biophys Res Commun 221:361–367
Swofford DL (1998) PAUP: phylogenetic analysis using parsimony (and other methods). Sinauer, Sunderland, Mass.
Thompson JD, Gibson TJ, Plewniak F, Jeanougin F, Higgins DG (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequences alignment aided by quality analysis tools. Nucleic Acids Res 25:4876–4882
Tsang V, Brand JA, Boyer A (1989) An enzyme-linked immunoelectrotransfer blot and glycoprotein antigens for diagnosing human cysticercosis (Taenia solium). J Infect Dis 159:50–59
Woese CR, Kandler O, Wheelis ML (1990) Towards a natural system of organisms: proposal for the domain Archaea, Bacteria and Eucarya. Proc Natl Acad Sci USA 87:4576–4579
Wool GI, Chan YL, Glück A (1995) Structure and evolution of mammalian ribosomal proteins. Biochem Cell Biol 73:933–947
Acknowledgements
This study was partially supported by grants IN218198 and IN213598 from the Programa de Apoyo a Proyectos de Investigación e Innovación Tecnológica of the Dirección General de Asuntos del Personal Académico, UNAM, and the Consejo Nacional de Ciencia y Tecnología grant 35333-M. The authors declare that the experiments performed in this work comply with the current ethical laws of the Universidad Nacional Autónoma de México.
Author information
Authors and Affiliations
Corresponding author
Additional information
Nucleotide sequences reported in this paper have been deposited in the GenBank database under the accession numbers AF225905 (Taenia solium ribosomal protein S15a cDNA), AY196206 and AY196207 (genomic DNA fragments from T. solium and T. saginata, respectively).
An erratum to this article can be found at http://dx.doi.org/10.1007/s00436-004-1089-5
Rights and permissions
About this article
Cite this article
Jiménez, L., Becerra, A. & Landa, A. Cloning, expression and partial characterization of a gene encoding the S15a ribosomal protein of Taenia solium . Parasitol Res 92, 414–420 (2004). https://doi.org/10.1007/s00436-003-1021-4
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00436-003-1021-4