Biopolym. Cell. 1997; 13(6):474-478.
http://dx.doi.org/10.7124/bc.0004A9
Structure and Function of Biopolymers
Homology of C-terminal non-catalytic domain of mammalian tyrosyl-tRNA synthetase with cylokine EMAP II and non-catalytic domains of methionyl- and phenylalanyl-tRNA synthetases
1Levanets O. V., 1Naidenov V. G., 1Odynets K. A., 1Woodmaska M. I., 1Matsuka G. Kh., 1Kornelyuk A. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Mammalian tyrosyl-tRNA synthetase contains C-terminal domain which is dispensable for the enzyme catalytic activity in the. aminoacylation of homologous tRNATyr. Cloning and sequencing cDNA which encodes this mammalian tyrosyl-tRNA synthetase was performed by the 3'-RACE method. Comparison of the amino acid sequence of the C-terminal domain of this mammalian tyrosyl-tRNA synthetase with other proteins using program BLASTP has shown the highest homology level (62.7 % identity) with a new cytokine, EMAP II, inducible by chemical cancerogenesis and corresponding to the p43 protein from high molecular weight aaRS complex of mammalians and also with non-catalytic C-terminal domains of methionyl-tRNA synthetases from nematode (62.7 %) and bacteria (27.7 %) and with N-terminal domain of the β-subunit of phenylalanyl-tRNA synthetase of E. coli (26.7 %). The hypothesis was proposed about possible forming of isolated C-domain as a result of the proteolytic digestion of tyrosyl-tRNA synthetase by intracellular proteases and about possible cytokinc-like activity of this C-domain.
Full text: (PDF, in Russian)

References

[1] Mirande M. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog Nucleic Acid Res Mol Biol. 1991;40:95-142.
[2] Kisselev LL, Wolfson AD. Aminoacyl-tRNA synthetases from higher eukaryotes. Prog Nucleic Acid Res Mol Biol. 1994;48:83-142.
[3] Cirakoglu B, Waller JP. Do yeast aminoacyl-tRNA synthetases exist as soluble enzymes within the cytoplasm? Eur J Biochem. 1985;149(2):353-61.
[4] Korneliuk AI, Kurochkin IV, Matsuka GKh. Tyrosyl-tRNA synthetase from the bovine liver. Isolation and physico-chemical properties. Mol Biol (Mosk). 1988;22(1):176-86.
[5] Gnatenko DV, Korneliuk AI, Kurochkin IV, Ribkinska TA, Matsuka GKh. Isolation and characteristics of functionally active proteolytically modified forms of tyrosyl-tRNA synthetase from bovine liver. Ukr Biokhim Zh. 1991;63(4):61-7.
[6] Kurochkin IV, Korneliuk AI, Matsuka GKh. Interaction of eukaryotic tyrosyl-tRNA-synthetase with high molecular weight RNA. Mol Biol (Mosk). 1991;25(3):779-86.
[7] Levanets OV, Naidenov VG, Woodmaska MI, Matsuka GH, Kornelyuk AI. Cloning of cDNA encoding C-terminal part of mammalian tyrosyl-tRNA synthetase using of PCR-amplified radioactive probe. Biopolym. Cell. 1997; 13(2):121-6.
[8] Kao J, Ryan J, Brett G, Chen J, Shen H, Fan YG, Godman G, Familletti PC, Wang F, Pan YC, et al. Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms. J Biol Chem. 1992;267(28):20239-47.
[9] Kao J, Houck K, Fan Y, Haehnel I, Libutti SK, Kayton ML, Grikscheit T, Chabot J, Nowygrod R, Greenberg S, et al. Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II. J Biol Chem. 1994;269(40):25106-19.
[10] Tas MP, Murray JC. Endothelial-monocyte-activating polypeptide II. Int J Biochem Cell Biol. 1996;28(8):837-41.
[11] Dardel F, Fayat G, Blanquet S. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene. J Bacteriol. 1984;160(3):1115-22.
[12] Mechulam Y, Fayat G, Blanquet S. Sequence of the Escherichia coli pheST operon and identification of the himA gene. J Bacteriol. 1985;163(2):787-91.
[13] Frohman MA, Dush MK, Martin GR. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci U S A. 1988;85(23):8998-9002.
[14] Maniatis T, Fritsch EF, Sambrook J. Molecular cloning: a laboratory manual. New York: Cold Spring Harbor Lab, 1982; 545 p.
[15] Costa GL, Grafsky A, Weiner MP. Cloning and analysis of PCR-generated DNA fragments. PCR Methods Appl. 1994;3(6):338-45.
[16] Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977;74(12):5463-7.
[17] Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol. 1990;215(3):403-10.
[18] Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P. Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. Proc Natl Acad Sci U S A. 1996;93(1):166-70.
[19] Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O, et al. Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. Nature. 1995;377(6547 Suppl):3-174.
[20] Wilson R, Ainscough R, Anderson K, Baynes C, Berks M, Bonfield J, Burton J, Connell M, Copsey T, Cooper J, et al. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature. 1994;368(6466):32-8.
[21] Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG, Blake JA, FitzGerald LM, Clayton RA, Gocayne JD, Kerlavage AR, Dougherty BA, Tomb JF, Adams MD, Reich CI, Overbeek R, Kirkness EF, Weinstock KG, Merrick JM, Glodek A, Scott JL, Geoghagen NS, Venter JC. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 1996;273(5278):1058-73.
[22] Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 1996;15(19):5437-48.
[23] Keller B, Kast P, Hennecke H. Cloning and sequence analysis of the phenylalanyl-tRNA synthetase genes (pheST) from Thermus thermophilus. FEBS Lett. 1992;301(1):83-8.
[24] Himmelreich R, Hilbert H, Plagens H, Pirkl E, Li BC, Herrmann R. Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res. 1996;24(22):4420-49.
[25] Cassio D, Waller JP. Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme. Eur J Biochem. 1971;20(2):283-300.
[26] Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. Nat Struct Biol. 1995;2(7):537-47.
[27] Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Structure. 1997;5(1):59-68.
[28] Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science. 1986;234(4774):364-8.
[29] Jacobo-Molina A, Villa-Garcia M, Chen HC, Yang DC. Proteolytic signal sequences (PEST) in the mammalian aminoacyl-tRNA synthetase complex. FEBS Lett. 1988;232(1):65-8.