Abstract
A full-length cDNA encoding translationally controlled tumor protein of marine flatfish turbot (Scophthalmus maximus), SmTCTP, was isolated with rapid amplification of cDNA Ends (RACE). SmTCTP consisted of a 5′ untranslated region (UTR) of 84 bp, a 3′ UTR of 451 bp and an open reading frame (ORF) of 513 bp, encoding a protein of 170 amino acid residues, which contained two signature sequences of TCTP family. The 5′UTR of SmTCTP started with a 5′-terminal oligopyrimidine tract (5′-TOP), a typical feature for translationally controlled mRNAs. The deduced amino acid sequence of SmTCTP was similar to the other known vertebrate TCTPs in a range of 58.8% to 64.1%. The length of fish TCTPs was diverse among species, e.g., TCP of turbot and sea perch (Lateolabrax japonicus) is 170 aa in length, while that of zebrafish (Danio rerio) and rohu (Labeo rohita) is 171 aa in length. Northern blot analysis revealed that SmTCTP has only one type of mRNA. Its expression level in albino skin was slightly higher than that in normal skin. We constructed the pET30a-SmTCTP expression plasmid. The recombinant protein of His-tag SmTCTP was over-expressed in E. coli, purified and identified with peptide mass fingerprinting. These results may pave the way of further investigation of the biological function of TCTP in fish.
Similar content being viewed by others
References
Bairoch, A., P. Bucher, and K. Hofmann, 1997. The PROSITE database, its status in 1997. Nucleic Acids Res., 25: 217–221.
Bangrak, P., P. Graidist, W. Chotigeat, and A. Phongdara, 2004. Molecular cloning and expression of a mammalian homologue of a translationally controlled tumor protein (TCTP) gene from Penaeus monodon shrimp. J. Biotechnol., 108: 219–226.
Bheekha-Escura, R., D. W. MacGlashan, J. M. Langdon, and S. M. MacDonald, 2000. Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-3D10. Blood, 96: 2191–2198.
Bhisutthibhan, J., X. Q. Pan, P. A. Hossler, D. J. Walker, C. A. Yowell, J. Carlton, et al., 1998. The Plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin. J. Biol. Chem., 273: 16 192–16 198.
Bolker, J. A., and C. R. Hill, 2000. Pigmentation development in hatchery-reared flatfishes. J. Fish Biol., 56: 1029–1052.
Bommer, U. A., and B. J. Thiele, 2004. The translationally controlled tumour protein (TCTP). Int. J. Biochem. Cell Biol., 36: 379–385.
Bonnet, C., E. Perret, X. Dumont, A. Picard, D. Caput, and G. Lenaers, 2000. Identification and transcription control of fission yeast genes repressed by an ammonium starvation growth arrest. Yeast, 16: 23–33.
Cans, C., B. J. Passer, V. Shalak, V. Nancy-Portebois, V. Crible, N. Amzallag, et al., 2003. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc. Natl. Acad. Sci. U. S. A., 100: 13 892–13 897.
Cheng, W., L. Guo, Z. Zhang, H. M. Soo, C. Wen, W. Wu, et al., 2006. HNF factors form a network to regulate liver-enriched genes in zebrafish. Dev. Biol., 294: 482–496.
Chung, S., M. Kim, W. Choi, J. Chung, and K. Lee, 2000. Expression of translationally controlled tumor protein mRNA in human colon cancer. Cancer Lett., 156: 185–190.
Gachet, Y., S. Tournier, M. Lee, A. Lazaris-Karatzas, T. Poulton, and U. A. Bommer, 1999. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J. Cell Sci., 112: 1257–1271.
Gross, B., M. Gaestel, H. Bohm, and H. Bielka, 1989. cDNA sequence coding for a translationally controlled human tumor protein. Nucleic Acids Res., 17: 8367.
Guo, H. R., B. Huang, S. C. Zhang, and F. Qi, 2003. Biochemical and histochemical activities of tyrosinase in the skins of normal and albino turbot Scophthalmus maximus. Fish Physiol. Biochem., 29: 67–76.
Jung, J., M. Kim, M. J. Kim, J. Kim, J. Moon, J. S. Lim, et al., 2004. Translationally controlled tumor protein interacts with the third cytoplasmic domain of Na,K-ATPase alpha subunit and inhibits the pump activity in HeLa cells. J. Biol. Chem., 279: 49868–49875.
Kakuturu, V. N. R., C. Lin, G. Munirathinam, and R. Kalyanasundaram, 2002. Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni. J. Biol. Chem., 277: 31207–31213.
Kang, H. S., M. J. Lee, H. Song, S. H. Han, Y. M. Kim, J. Y. Im, et al., 2001. Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J. Immunol., 166: 6545–6554.
Kim, M., Y. Jung, K. Lee, and C. Kim, 2000. Identification of the calcium binding sites in translationally controlled tumor protein. Arch. Pharm. Res., 23: 633–636.
Liu, H., H. W. Peng, Y. S. Cheng, H. S. Yuan, and H. F. Yang-Yen, 2005. Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol. Cell. Biol., 25: 3117–3126.
MacDonald, S. M., J. Bhisutthibhan, T. A. Shapiro, S. J. Rogerson, T. E. Taylor, M. Tembo, et al., 2001. Immune mimicry in malaria, Plasmodium falciparum secretes a functional histamine-releasing factor homolog in vitro and in vivo. Proc Natl. Acad. Sci. U. S. A., 98: 10 829–10 832.
MacDonald, S. M., T. Rafnar, J. Langdon, and L. M. Lichtenstein, 1995. Molecular identification of an IgE-dependent histamine-releasing factor. Science, 269: 688–690.
Meyuhas, O., D. Avni, and S. Shama, 1996. Translational control of ribosomal protein mRNAs in eukaryotes. In: Translational Control. Hershey, J. B., et al., eds., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 363–388.
Nielsen, H. V., A. H. Johnsen, J. C. Sanchez, D. F. Hochstrasser, and P. O. Schiotz, 1998. Identification of a basophil leukocyte interleukin-3-regulated protein that is identical to IgE-dependent histamine-releasing factor. Allergy, 53: 642–652.
Perkins, D. N., D. J. Pappin, D. M. Creasy, and J. S. Cottrell, 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis, 20: 3551–3567.
Qiu, L. H., L. S. Song, L. T. Wu, W. Xu, and S. G. Jiang, 2005. cDNA cloning and mRNA expression of the translationally controlled (Lateolabrax japonicus). Acta Oceanol. Sin., 24: 113–119.
Sambrook, J., E. F. Fritsch, and T. Maniatis, 1989. Molecular Cloning: A Laboratory Mannal. 2nd ed. Cold Spring Harbor Laboratory Press, USA. 22–50.
Sanchez, J. C., D. Schaller, F. Ravier, O. Golaz, S. Jaccoud, M. Belet, et al., 1997. Translationally controlled tumor protein, a protein identified in several nontumoral cells including erythrocytes. Electrophoresis, 18: 150–155.
Thaw, P., N. J. Baxter, A. M. Hounslow, C. Price, J. P. Waltho, and C. J. Craven, 2001. Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nat. Struct. Biol., 8: 701–704.
Thiele, H., M. Berger, A. Skalweit, and B. J. Thiele, 2000. Expression of the gene and processed pseudogenes encoding the human and rabbit translationally controlled tumour protein (TCTP). Eur. J. Biochem., 267: 5473–5481.
Tuynder, M., G. Fiucci, S. Prieur, A. Lespagnol, A. Geant, S. Beaucourt, et al., 2004. Translationally controlled tumor protein is a target of tumor reversion. Proc. Natl. Acad. Sci. U.S.A., 101: 15 364–15 369.
Venizelos, A., and D. D. Benetti, 1999. Pigment abnormalities in flatfish. Aquaculture, 176: 181–188.
Venugopal, T., 2005. Evolution and expression of translationally controlled tumour protein (TCTP) of fish. Comp. Biochem. & Physiol. Part B: Biochem. & Mol. Biol., 142: 8–17.
Xu, A., A. R. Bellamy, and J. A. Taylor, 1999. Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level. Biochem. J., 342: 683–689.
Yarm, F. R., 2002. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Mol. Cell Biol., 22: 6209–6221.
Yenofsky, R., I. Bergmann, and G. Brawerman, 1982. Messenger RNA species partially in a repressed state in mouse sarcoma ascites cells. Proc. Natl. Acad. Sci. U.S.A., 79: 5876–5880.
Yenofsky, R., S. Cereghini, A. Krowczynska, and G. Brawerman, 1983. Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol. Cell Biol., 3: 1197–1203.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Wang, J., Guo, H., Zhang, S. et al. Cloning, expression and characterization of translationally controlled tumor protein (TCTP) gene from flatfish turbot (Scophthalmus maximus). J. Ocean Univ. China 7, 184–192 (2008). https://doi.org/10.1007/s11802-008-0184-0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11802-008-0184-0