Biopolym. Cell. 1996; 12(5):21-28.
http://dx.doi.org/10.7124/bc.000444
Autoantibodies directed against tyrosyl-tRNA synthetase modulate its aminoacylating activity
1Sidorik L. L., 1Rodnin N. V., 1Savinskaya L. A., 1Ribkinska T. A., 1Rozhko O. T., 1Korneliuk A. I., 1Matsuka G. H.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The autoantibodies directed against many proteins and ribonucleoproteids, the components of translation apparatus, have been detected at several systemic autoimmune diseases. Earlier we revealed the autoantibodies against seryl-tRNA synthetase in the blood sera of patients with systemic lupus erythematosus and rheumatoid arthritis. In the present paper we report about the autoantibodies directed against tyrosyl-tRNA synthetase, the other translation apparatus component. While the polyclonal antibodies inhibited the aminoacylating activity of TyrRS down to 30 % the autoantibodies from autoimmune sera activated it up to 280 % that hasn't been observed for any other synthetase. The possible reasons of this phenomenon are discussed.
Full text: (PDF, in Russian)

References

[1] Kisselev LL, Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.
[2] Schimmel P. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu Rev Biochem. 1987;56:125-58.
[3] Kiselev LL. Aminoacyl-tRNA synthetases (codases) and their noncanonical functions. Mol Biol (Mosk). 1990;24(6):1445-73. PubMed
[4] Popenko VI, Cherni NE, Beresten' SF, Zargarova TA, Favorova OO. Immune electron microscope determination of the localization of tryptophanyl-tRNA-synthetase in bacteria and higher eukaryotes. Mol Biol (Mosk). 1989;23(6):1669-81.
[5] Sidorik LL, Popenko VI, Cherny NE, Tukalo MA, Beresten SF, Matsuka GKh. Immunoelectron-microscopic study of seryl-tRNA-synthetase localization in cells of higher eucaryotes. Biopolym Cell. 1990;6(5):72-7.
[6] Avrameas S. Natural autoantibodies: from 'horror autotoxicus' to 'gnothi seauton'. Immunol Today. 1991;12(5):154-9.
[7] Chan EK, Tan EM. Human autoantibody-reactive epitopes of SS-B/La are highly conserved in comparison with epitopes recognized by murine monoclonal antibodies. J Exp Med. 1987;166(6):1627-40.
[8] Tan EM, Reimer G, Sullivan K. Intracellular autoantigens: Diagnostic fingerprints but aetiological dilemmas. Ciba foundation symp. «Autoimmunity and Autoimmune Disease». Chichester: Wiley, 1987: 25-42.
[9] Mathews MB, Bernstein RM. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature. 1983 Jul 14-20;304(5922):177-9.
[10] Targoff IN. Autoantibodies in polymyositis. Antinuclear antibodies. New York: Acad, press, 1993. 686 p.
[11] Mathews MB, Reichlin M, Hughes GR, Bernstein RM. Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody. J Exp Med. 1984;160(2):420-34.
[12] Bunn CC, Bernstein RM, Mathews MB. Autoantibodies against alanyl-tRNA synthetase and tRNAAla coexist and are associated with myositis. J Exp Med. 1986;163(5):1281-91.
[13] Bunn CC, Mathews MB. Autoreactive epitope defined as the anticodon region of alanine transfer RNA. Science. 1987;238(4830):1116-9.
[14] Targoff IN. Autoantibodies to aminoacyl-transfer RNA synthetases for isoleucine and glycine. Two additional synthetases are antigenic in myositis. J Immunol. 1990;144(5):1737-43.
[15] Vartanian OA. Detection of autoantibodies against phenylalanyl-, tyrosyl-, and tryptophanyl-tRNA-synthetase and anti-idiotypic antibodies to it in serum from patients with autoimmune diseases. Mol Biol (Mosk). 1991;25(4):1033-9.
[16] Ribkinska TA, Kornelyuk AI, Beresten SF, Matsuka GKh. The immunochemical approach for studies of structure tyrosyl-tRNA synthetase from bovine liver. Biopolym Cell. 1991; 7(5):33-6.
[17] 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.
[18] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[19] Bobik VI, Veberov AV, Ryabenko DV, Dubrovskaya GV, Rodnin NV, Sidorik LL. The purification of the main tissue-specific antigens from the normal and effected by dilatative cardiomyopathia human heart. Biopolym Cell. 1993;9(6):63-6.
[20] Ternynck T, Bleux C, Gregoire J, Avrameas S, Kanellopoulos-Langevin C. Comparison between autoantibodies arising during Trypanosoma cruzi infection in mice and natural autoantibodies. J Immunol. 1990;144(4):1504-11.
[21] Bailey GS. The production of antisera. Meth Mol Biol. 1984: 295-300.
[22] Gudzera OI, Sidorik LL, Zolotukhina IV, Tukalo MA, Matsuka GKh. Isolation of seryl-tRNA synthetase from the animal liver by proximate method. Biopolym Cell. 1990; 6(2):105-7.
[23] Sidorik LL, Gudzera OI, Dragovoz VA, Tukalo MA, Beresten SF. Immuno-chemical non-cross-reactivity between eukaryotic and prokaryotic seryl-tRNA synthetases. FEBS Lett. 1991;292(1-2):76-8.
[24] Beresten' SF, Filonenko VV, Favorova OO. Immunochemical study of tryptophanyl-tRNA-synthetase. Biokhimiia. 1991;56(7):1155-89.
[25] Sidorik LL. Seryl-tRNA synthetase – a novel autoantigen during systemic autoimmune diseases. Biopolym Cell. 1994;10(3-4):68-74.
[26] Dang CV, Dang CV. Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states. Mol Cell Biochem. 1986;71(2):107-20.