Аміноацил-тРНК синтетази вищих еукаріот при змінах стану організму

Іванов, Л. Л.

doi:10.7124/bc.000332

Biopolym. Cell. 1992; 8(5):3-11.

http://dx.doi.org/10.7124/bc.000332

Огляди

Аміноацил-тРНК синтетази вищих еукаріот при змінах стану організму

1Іванов Л. Л.

Інститут молекулярної біології і генетики НАН України
Вул. Академіка Заболотного, 150, Київ, Україна, 03680

Abstract

В огляді узагальнено експериментальні результати вивчення активності і властивостей аміноацил-тРНК синтетаз (АРСаз) при різних фізіологічних і патологічних станах вищих еукаріотичних організмів. Розглянуто питання кореляції між рівнем біосинтезу білка в органах і активністю АРСаз. Проаналізовано дані про стабільність високомолекулярних комплексів АРСаз при зміні стану огранізму

Повний текст: (PDF, російською)

References

[1] El'skaya A. V., Starodub N. F., Potapov A. P., Kovalenko M. I., Ovcharenko G. V., Obolenskaya M. U., Ivanov L. L. Regulation of protein biosynthesis in eukaryotes Kiev: Nauk. dumka, 1990 280 p.

[2] Kisselev LL, Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.

[3] Dang CV, Dang CV. Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic. Biochem J. 1986;239(2):249-55.

[4] 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.

[5] Usatenko MS, Teslenko LV. Regulation by insulin of the activity of aminoacyl-tRNA synthetases in intact and denervated rabbit muscles. Biokhimiia. 1978;43(12):2196-9.

[6] Damuni Z, Caudwell FB, Cohen P. Regulation of the aminoacyl-tRNA synthetase complex of rat liver by phosphorylation/dephosphorylation in vitro and in vivo. Eur J Biochem. 1982;129(1):57-65.

[7] Berg BH. The early influence of 17-beta-oestradiol on 17 aminoacyl-tRNA synthetases of mouse uterus and liver. Phosphorylation as a regulation mechanism. Biochim Biophys Acta. 1977;479(2):152-71.

[8] Arafat W, Kern D, Dirheimer G. Inhibition of aminoacyl-tRNA synthetases by the mycotoxin patulin. Chem Biol Interact. 1985;56(2-3):333-49.

[9] Wagner G, Unterreiner AM. Inhibition of rat liver aminoacyl-tRNA synthetases in vitro after acute and chronic aflatoxin B1 administration in vivo. Chem Biol Interact. 1981;37(1-2):233-44.

[10] Creppy EE, Kern D, Steyn PS, Vleggaar R, Röschenthaler R, Dirheimer G. Comparative study of the effect of ochratoxin A analogues on yeast aminoacyl-tRNA synthetases and on the growth and protein synthesis of hepatoma cells. Toxicol Lett. 1983;19(3):217-24.

[11] Roth A, Creppy EE, Kane A, Bacha H, Steyn PS, Röschenthaler R, Dirheimer G. Influence of ochratoxin B on the ochratoxin A inhibition of phenylalanyl-tRNA formation in vitro and protein synthesis in hepatoma tissue culture cells. Toxicol Lett. 1989;45(2-3):307-13.

[12] Yaremchuk AD, Goncharov NI, Bogdanaite OD, Kondratyuk TP, Tarasevichene LV, El'skaya AV. Aminoacyl-tRNA synthetases complexes under sharp changes in protein biosynthesis. Doklady Akad Nauk Ukr SSR. Ser B. 1984 3(3):82–5.

[13] Sushkova VV, Kas'ianova NN, Vasil'eva SM, Gulyĭ MV. The effect of ethanol on the initial stage of protein biosynthesis in the rat liver. Vopr Med Khim. 1988;34(4):21-4.

[14] Sushkova VV, Kasiyanova NM, Gulyy MF. Change in the initial stages of protein biosynthesis and aminoacyl-tRNA synthetase activity in the liver of animals as affected by ethanol and acetaldehyde. Doklady Akad Nauk Ukr SSR. Ser B. 1989;(8):81-3.

[15] Mäenpää PH, Tewari S. A change in isoaccepting leucine transfer RNA species in rat brain after prolonged ingestion of ethanol. Med Biol. 1983;61(6):313-8.

[16] Gantt JS, Bennett CA, Arfin SM. Increased levels of threonyl-tRNA synthetase in a borrelidin-resistant Chinese hamster ovary cell line. Proc Natl Acad Sci U S A. 1981;78(9):5367-70.

[17] Gerken SC, Arfin SM. Chinese hamster ovary cells resistant to borrelidin overproduce threonyl-tRNA synthetase. J Biol Chem. 1984;259(14):9202-6.

[18] Hasegawa K, Omata S, Sugano H. In vivo and in vitro effects of methylmercury on the activities of aminoacyl-tRNA synthetases in rat brain. Arch Toxicol. 1988;62(6):470-2.

[19] Bölöni E. Studies on the valyl-h-tRNA synthetase of chick embryo brain irradiated with 60Co gamma-rays, in vivo. Int J Radiat Biol Relat Stud Phys Chem Med. 1980;37(1):61-9.

[20] Bölöni E, Batke I, Szabó LD. Difference in radiosensitivity of valyl-tRNA synthetases isolated from chick embryo liver and brain. Int J Radiat Biol Relat Stud Phys Chem Med. 1984;45(4):359-69.

[21] Bölöni E. Valyl-tRNA synthetase from chick embryo brain. Properties of the sulfhydryl groups. Acta Biochim Biophys Acad Sci Hung. 1979;14(4):259-70.

[22] Verkhogliad IN, Vinogradova RP, Kucherenko NE. Study of the kinetics of thermoinactivation of lysyl-tRNA-synthetase from the liver of x-irradiated rats. Radiobiologiia. 1985;25(2):185-90.

[23] Verkhogliad IN, Dragan AI, Vinogradova RP, Kucherenko NE. Effect of roentgen irradiation on the luminescent properties of rat liver lysyl-tRNA synthetase. Radiobiologiia. 1984;24(6):748-52.

[24] Vinogradova RP, Kucherenko NE, Demchenko IB. Effect of ionizing radiation on methylation of lysyl tRNA synthetase from rat liver. Radiobiologiia. 1986;26(1):88-91.

[25] Sleptsova IL, Demchenko IB, Vinogradova RP. Properties methyltransferase multienzyme complex aminoacyl-tRNA synthetases of the rat liver. Probl. obshch. i molekulyar. biologii. 1985;4: 14-8.

[26] Vinogradova RP, Kucherenko NE, Verkhogliad IN, Mirutenko NV. Phosphorylation of lysyl tRNA synthetase from the liver of rats exposed to x-rays. Radiobiologiia. 1982;22(4):446-9.

[27] Glushak VN, Demchenko AP, Orlovskaia NN, Gulyĭ MF. Spectral characteristics of muscle aspartyl- and valyl-tRNA- synthetases and their complexes with substrates in normal conditions and after prolonged starvation. Ukr Biokhim Zh. 1984;56(5):519-26.

[28] Gulyĭ MF, Orlovskaia NN, Veselovskaia LD. Characteristics of the structure and specificity of aspartyl- and valyl-tRNA-synthetases from muscle tissue of long-fasting rabbits. Ukr Biokhim Zh. 1987;59(5):32-6.

[29] Ilan J. Similarities in properties and a functional defference in purified leucyl-tRNA synthetase isolated from two developmental stages of Tenebrio molitor. Dev Biol. 1975;42(1):64-74.

[30] Sallafranque ML, Garret M, Benedetto JP, Fournier M, Labouesse B, Bonnet J. Tryptophanyl-tRNA synthetase is a major soluble protein species in bovine pancreas. Biochim Biophys Acta. 1986;882(2):192-9.

[31] Demidov SV, El'skaia AB. Aminoacyl-tRNA-synthetase activity in rabbit liver tissue during ontogenesis. Ukr Biokhim Zh. 1980;52(1):75-8.

[32] Bublitz C. Some properties of proline-sRNA synthetase from rat liver. Biochim Biophys Acta. 1966;128(1):165-71.

[33] Gabius HJ, Gabius S, Graupner G, Cramer F, Rehm S. Aminoacyl-tRNA synthetases in liver, spleen and small intestine of aged leukemic and aged normal mice. Z Naturforsch C. 1983;38(9-10):881-2.

[34] Gabius HJ, Graupner G, Cramer F. Activity patterns of aminoacyl-tRNA synthetases, tRNA methylases, arginyltransferase and tubulin: tyrosine ligase during development and ageing of Caenorhabditis elegans. Eur J Biochem. 1983;131(1):231-4.

[35] Takahashi R, Mori N, Goto S. Alteration of aminoacyl tRNA synthetases with age: accumulation of heat-labile enzyme molecules in rat liver, kidney and brain. Mech Ageing Dev. 1985;33(1):67-75.

[36] Takahashi R, Goto S. Age-associated accumulation of heat-labile aminoacyl-tRNA synthetases in mice and rats. Arch Gerontol Geriatr. 1987;6(1):73-82.

[37] Goto S, Takahashi R. Accumulation of heat-labile aminoacyl-tRNA synthetases and effects of dietary restriction in aged mice. Age. 1987; 10(3): 120.

[38] Takahashi R, Goto S. Alteration of aminoacyl-tRNA synthetase with age: heat-labilization of the enzyme by oxidative damage. Arch Biochem Biophys. 1990;277(2):228-33.

[39] Jayabaskaran C, Kuntz M, Guillemaut P, Weil JH. Variations in the Levels of Chloroplast tRNAs and Aminoacyl-tRNA Synthetases in Senescing Leaves of Phaseolus vulgaris. Plant Physiol. 1990;92(1):136-40.

[40] Elska A, Matsuka G, Matiash U, Nasarenko I, Semenova N. tRNA and aminoacyl-tRNA synthetases during differentiation and various functional states of the mammary gland. Biochim Biophys Acta. 1971;247(3):430-40.

[41] El'skaya AV. Transfer RNA and aminoacyl-tRNA synthetases in the regulation of protein biosynthesis at translational level. Sov. Sci. Rev. D. Physicochem. Biol. 1988; 28(1):149-84.

[42] Del Monte U, Capaccioli S, Neri Cini G, Perego R, Caldini R, Chevanne M. Effects of liver regeneration on tRNA contents and aminoacyl-tRNA synthetase activities and sedimentation patterns. Biochem J. 1986;236(1):163-9.

[43] Iaremchuk AD, Tarasiavichene LE, Kondratiuk TP, El'skaia AV. Aminoacyl-tRNA-synthetases and their high molecular weight complexes in the regenerating rat liver. Mol Biol (Mosk). 1984;18(5):1336-41.

[44] El'skaya AV, Yaremchuk AD, Goncharov NI, Buldakova OV. Study of the functional role of macromolecular complexes of aminoacyl-tRNA synthetases. Probl. curr biochem biotechnol: Proc. of reports. Combine 8. symposium. biochem. soc. USSR and GDR: Riga 1985: 169-170.

[45] Gabius HJ, Goldbach S, Graupner G, et al. OAminoacyl-tRNA synthetases in ageing and leukemia (EC6.1.1). Hoppe-Seyler's Zeitschurift fur physiologische chemie. 1982; 363(9): 874

[46] Agris PF, Woolverton DK, Setzer D. Subcellular localization of S-adenosyl-L-methionine:tRNA methyltransferases with aminoacyl-tRNA synthetases in human and mouse: normal and leukemic leukocytes. Proc Natl Acad Sci U S A. 1976;73(11):3857-61.

[47] del Monte U, Neri Cini G, Capaccioli S et al. Studies on particulate and soluble forms of aminoacyl-tRNA synthetases from rat liver and hepatomas. Med Biol Environ. 1981; 9(1):375-9.

[48] Perego R, del Monte U. Allotropism in aminoacyl-tRNA synthetases from Yoshida hepatoma AH130. IRCS Med Sci. 1982; 10: 536-7.

[49] Del Monte U, Perego R. Multiple forms of glutaminyl-tRNA synthetase in rat hepatoma induced by 4-dimethylaminoozobenzene. Med Biol Environ. 1983; 11(1): 151-6.

[50] Perego R, Delmonte U. A stable complex from Yoshida ascites hepatoma AH 130 containing nine aminoacyl-tRNA synthetases. Cell Biol Int Rep. 1986;10(6):477.

[51] Thomas K, Scheets K, Allen S, Hedgcoth C. Comparison of complexes containing lysyl-tRNA synthetase from normal and virus-transformed cells. Can J Biochem. 1982;60(8):804-10.

[52] Tamuliavichius AI, Ivanov LL, Lukoshiavichius LIu, Prashkiavichius AK. Aminoacyl-tRNA synthetases and their high molecular weight complexes in autolysis of the swine heart. Vopr Med Khim. 1985;31(5):104-7.

[53] Ivanov LL, Tamuliavichius AA, Lukoshiavichius LIu, Kovalenko MI, Rodovichius GA. Aminoacyl-tRNA-synthetases and their high molecular weight complexes in experimental myocardial ischemia. Mol Biol (Mosk). 1984;18(5):1326-9.

[54] Kashauskas AP, Tamuliavichius AA, Lukoshiavichius LIu, Ivanov LL, Prashkiavichius AK. Biological activity of tRNA and aminoacyl-tRNA-synthetases from the swine myocardium in anoxia and subsequent reoxygenation. Vopr Med Khim. 1988;34(2):84-6.

[55] Stapulenis RR, Ivanov LL, Lukoshiavichius LIu, Daukantaĭte IS, Kondratas DZ, Prashkiavichius AK. Study of the properties of leucyl-tRNA synthetase from porcine myocardium in a normal state and in experimental ischemia. Vopr Med Khim. 1989;35(4):56-60.

[56] Lukoshiavichius LIu, Rodovichius GA, Kovalenko MM, Pivoriunaĭte II, Prashkiavichius AK. tRNA and aminoacyl-tRNA synthetases from the liver of rabbits in experimental myocardial infarction. Vopr Med Khim. 1983;29(4):65-9.

[57] Ivanov LL, Lukoshiavichius LIu, Kovalenko MI, Bagdonaĭte OD, Lekis AV. Amino acyl tRNA synthetase complexes in rabbit liver in experimental myocardial infarction. Ukr Biokhim Zh. 1983;55(4):368-71.

[58] Ivanov LL, Martinkus ZP, Lekis AV, Lukoshiavichius LIu, Prashkiavichius AK. Distribution of aminoacyl-t-RNA-synthetase activity in rabbit liver cells during disruption of protein biosynthesis in experimental myocardia infarct. Ukr Biokhim Zh. 1989;61(2):34-8.

[59] Martinkus ZP, Ivanov LL, Lekis AV, Priashkiavichius AK. Role of aminoacyl-tRNA-synthetases in changes in the rate of protein biosynthesis in the rabbit liver during myocardial ischemia. Biull Eksp Biol Med. 1990;109(6):563-5.

[60] Martinkus ZP, Ivanov LL, Lekis AV, Lukoshiavichius AK, Prashkiavichius AK. Interaction of eukaryotic aminoacyl-tRNA-synthases with polyribosomes. Vopr Med Khim. 1990;36(5):6-8.

[61] Dang CV, Dang CV. Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states. Mol Cell Biochem. 1986;71(2):107-20.

[62] Lazard M, Mirande M, Waller JP. Expression of the aminoacyl-tRNA synthetase complex in cultured Chinese hamster ovary cells. Specific depression of the methionyl-tRNA synthetase component upon methionine restriction. J Biol Chem. 1987;262(9):3982-7.

[63] Enger MD, Ritter PO, Hampel AE. Altered aminoacyl-tRNA synthetase complexes in G1-arrested Chinese hamster ovary cells. Biochemistry. 1978;17(12):2435-8.

[64] Hampel AE, Ritter PO, Enger MD. A physically altered leucyl-tRNA synthetase complex in a CHO cell mutant. Nature. 1978 Dec 21-28;276(5690):844-5.

[65] Mansukhani A, Condon T, Hampel A, Oxender DL. A Chinese hamster ovary leucyl-tRNA synthetase mutant with a uniquely altered high molecular weight leucyl-tRNA synthetase complex. Biochem Genet. 1984;22(3-4):349-55.

[66] Klekamp M, Pahuski E, Hampel A. Reformation of leucyl-tRNA synthetase complexes in revertants from CHO mutant tsH1. Somatic Cell Genet. 1981;7(6):725-35.

[67] Pahuski E, Klekamp M, Condon T, Hampel AE. Altered aminoacyl-tRNA synthetase complexes in CHO cell mutants. J Cell Physiol. 1983;114(1):82-7.

[68] Mirande M, Le Corre D, Waller JP. A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex. Eur J Biochem. 1985;147(2):281-9.

[69] Maskoliunas RK, Liekis AV, Kovalenko MI. Protein biosynthesis in the cell-free protein-synthesizing systems from rabbit myocardium during total ischemia. Biopolym Cell. 1989; 5(1):84-6.

[70] Kasauskas A, Tamulevicius A-A, Rodovicius H. Protein synthesis in anoxic pig myocardium. J Mol Cell Cardiol. 1990;22:S66.

[71] Lekis AV, Buldakova OV, Kovalenko MI, Lukoshiavichius LIu, Prashkiavichius AK. Protein-synthesizing function of the liver of rabbits in experimental myocardial infarct. Biull Eksp Biol Med. 1985;99(1):57-60.

[72] Lekis AV, Mashanauskas TK, Ivanov LL, Lukoshyavichyus L, Kunach VA, Kovalenko MI, Prashkyvichyus A, Elskaya AV. Cultured polyscias-filicifolia bailey cell biomass stimulates protein-biosynthesis in rabbit liver. Khim farm zh. 1988; 22(8):970-3.

[73] Tarasiavichene LE, Iasaĭtis AA, Rachiauskaĭte DV, Ivanov LL, Prashkiavichius AK. Comparative characteristics of tRNA-methyltransferases from rabbit liver and myocardium under normal conditions and in experimental ischemia. Biokhimiia. 1989;54(3):427-33.

[74] Stapulionis RR, Ivanov LL, Lukosevicius LJ, Yarmolenko VV, Praskevicius AK. Purification and properties of two forms of leucyl-tRNA synthetase from pig myocardium. Biopolym Cell. 1986; 2(6):302-7.

[75] Dang CV. High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation. Biochem Biophys Res Commun. 1982;106(1):44-7.

[76] Molnar SJ, Rauth AM. The effect of amino acids on the temperature sensitive phenotype of the mammalian leucyl-tRNA synthetase mutant tsHl and its revertants. J Cell Physiol. 1979;98(2):315-26.