Biopolym. Cell. 1991; 7(1):63-69.
Structure and Function of Biopolymers
High molecular weight complex of tyrosyl-tRNA synthetase from bovine liver
1Gnatenko D. V., 1Kornelyuk A. I., 1Kurochkin I. V., 1Matsuka G. H.
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
Abstract
The tyrosyl-tRNA synthetase in postribosomal bovine liver supernatant is included as a compound of the high molecular weight complex with Mr > 106 Da. Dissociation of tyrosyl-tRNA synthetase from this complex due to proteolysis proceeds through the intermediate labile complex with Mr≈240 kDa. The thermostability of tyrosyl-tRNA synthetase at this intermediate labile complex is much higher in comparison with free enzyme. The labile intermediate complex of bovine liver tyrosyl-tRNA synthetase possesses the nonspecific affinity for high molecular weight ribosomal RNA.
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References
[1]
Kisselev LL., Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.
[2]
Dang CV, Johnson DL, Yang DC. High molecular mass amino acyl-tRNA synthetase complexes in eukaryotes. FEBS Lett. 1982;142(1):1-6.
[3]
Bandyopadhyay AK, Deutscher MP. Complex of aminoacyl-transfer RNA synthetases. J Mol Biol. 1971;60(1):113-22.
[4]
Cirakoglu B, Mirande M, Waller JP. A model for the structural organization of aminoacyl-tRNA synthetases in mammalian cells. FEBS Lett. 1985;183(2):185-90.
[5]
Dang CV, Dang CV. Multienzyme complexes of eukaryotic aminoacyl-tRNA synthetases. Biosci Rep. 1983;3(6):527–38.
[6]
Hampel A, Enger MD. Subcellular distribution of aminoacyl-transfer RNA synthetases in Chinese hamster ovary cell culture. J Mol Biol. 1973;79(2):285-93.
[7]
Roberts WK, Olsen ML. Studies on the formation and stability of aminoacyl-tRNA synthetase complexes from Ehrlich ascites cells. Biochim Biophys Acta. 1976;454(3):480-92.
[8]
Ritter PO, Enger MD, Hampel AE. Characterization of postribosomal aminoacyl-tRNA synthetases in cultured Chinese hamster ovary cells. Biochim Biophys Acta. 1979;562(3):377-85.
[9]
Vellekamp G, Sihag RK, Deutscher MP. Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form. J Biol Chem. 1985;260(17):9843-7.
[10]
Siddiqui FA, Yang DC. Generation of multiple forms of methionyl-tRNA synthetase from the multi-enzyme complex of mammalian aminoacyl-tRNA synthetases by endogenous proteolysis. Biochim Biophys Acta. 1985;828(2):177-87.
[11]
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.
[12]
Warburg O, Christian W. Isolierung und Kristallisation des Gärungsferments Enolase. Biochem J. 1941; 310(2):384-421.
[13]
Van Dang C, Yang DC. Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. Isolation and the structural relationship of synthetase complexes. J Biol Chem. 1979;254(12):5350-6.
[14]
Negrutskiĭ BS, El'skaia AV. Characteristic features of heat inactivation of leucyl-tRNA- synthetase from the rabbit liver in the presence of various tRNA conformers. Mol Biol (Mosk). 1984;18(5):1297-300.
[15]
Ovchinnikov LP, Seriakova TA, Avanesov AT, Alzhanova AT, Radzhabov HM, Spirin AS. RNA-binding proteins of rabbit reticulocytes. Isolation and electrophoretic characteristics. Eur J Biochem. 1978;90(3):517-25.
[16]
Prasada Rao YS, Srinivasan PR. Purification and properties of tyrosyl tRNA synthetase of rat liver. Nucleic Acids Res. 1977;4(11):3887-900.
[17]
Deák F, Dénes G. Purification and some properties of rat liver tyrosyl-tRNA synthetase. Biochim Biophys Acta. 1978;526(2):626-34.
[18]
Spirin AS, Ovchinnikov LP Compartmentalization of proteins in eukaryotic translation apparatus on polyribosomes. Prospects bioorgan, chemistry and molecular. biology. Nauka, 1986:59-67.
[19]
Kurochkin IV, Ribkinska TA, Gnatenko DV et al. Tyrosyl-tRNA synthetases from beef liver: generation of multiple enzyme forms by endogenous proteolysis. Int. seminar on interferon and biotechnol.: Abstr. Havana, 1989:S06-066.
[20]
Motorin YuA, Wolfson AD, Orlovsky AF, Gladilin KL. Purification of valyl-tRNA synthetase high-molecular-mass complex from rabbit liver. FEBS Lett. 1987;220(2):363-5.
[21]
Motorin YuA, Wolfson AD, Orlovsky AF, Gladilin KL. Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. FEBS Lett. 1988;238(2):262-4.
[22]
Fasiolo F, Gibson BW, Walter P, Chatton B, Biemann K, Boulanger Y. Cytoplasmic methionyl-tRNA synthetase from Bakers' yeast. A monomer with a post-translationally modified N terminus. J Biol Chem. 1985;260(29):15571-6.
