Biopolym. Cell. 1997; 13(1):18-21.
Structure and Function of Biopolymers
The use of polyamines for creation of effective reconstructed protein synthesizing system from rabbit liver
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
A cell-free reconstructed protein-synthesizing system from rabbit liver has been developed. The system contains highly purified homologous components of translation apparatus and is characterized by a sufficient rate of polypeptide synthesis. The use of spermine and spermidine has allowed to optimize the activity of the system at physiological concentration of Mg2+.
 Ugarova TYu. Eukaryotic cell-free protein synthesis system. Itogi nauki i tekhniki. VINITI (seria Mol. Biology; Vol. 7), 1976. 58-141.
 Rheinberger HJ, Nierhaus KH. The ribosomal E site at low Mg2+: coordinate inactivation of ribosomal functions at Mg2+ concentrations below 10 mM and its prevention by polyamines. J Biomol Struct Dyn. 1987;5(2):435-46.
 Bartetzko A, Nierhaus KH. Mg2+/NH4+/polyamine system for polyuridine-dependent polyphenylalanine synthesis with near in vivo characteristics. Methods Enzymol. 1988;164:650-8.
 Falvey AK, Staehelin T. Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits. J Mol Biol. 1970;53(1):1-19.
 Potapov AP, Ovcharenko GV, Soldatkin KA. Isolation and characterization of 40S-and 60S-ribosomal subunits from rabbit liver. Methods mol biol. Naukova dumka, 1986: 100-5.
 Keller EB, Zamecnik PC. The effect of guanosine diphosphate and triphosphate on the incorporation of labeled amino acids into proteins. J Biol Chem. 1956;221(1):45-59.
 Negrutskii BS, Budkevich TV, Shalak VF, Turkovskaya GV, El'Skaya AV. Rabbit translation elongation factor 1 alpha stimulates the activity of homologous aminoacyl-tRNA synthetase. FEBS Lett. 1996;382(1-2):18-20.
 Iwasaki K, Kaziro Y. Polypeptide chain elongation factors from pig liver. Methods Enzymol. 1979;60:657-76.
 Brunngraber EF. A simplified procedure for the preparation of "soluble" RNA from rat liver. Biochem Biophys Res Commun. 1962;8:1-3.
 Triana-Alonso FJ, Chakraburtty K, Nierhaus KH. The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J Biol Chem. 1995;270(35):20473-8.
 Zheltovskaya I, Turkovskaya GV, Yaremchuk AD, Elskaya AV. Eukaryotic tRNA-dependent cell-free protein synthesis system. Molecular Biology methods. : Coll scientific work. Kiev: Naukova Dumka, 1979: 90-98.
 Takeda Y. Polyamines and protein synthesis. I. The effect of polyamines on cell free polyphenylalanine synthesis in Escherichia coli. J Biochem. 1969;66(3):345-9.
 Atkins JF, Lewis JB, Anderson CW, Gesteland RF. Enhanced differential synthesis of proteins in a mammalian cell-free system by addition of polyamines. J Biol Chem. 1975;250(14):5688-95.
 Igarashi K, Eguchi K, Tanaka M, Hirose S. Effect of polyamines on isoleucyl-tRNA formation by rat-liver isoleucyl-tRNA synthetase. Eur J Biochem. 1978;82(1):301-7.
 Igarashi K, Sugawara K, Izumi I, Nagayama C, Hirose S. Effect of polyamines of polyphenylalanine synthesis by Escherichia coli and rat-liver ribosomes. Eur J Biochem. 1974;48(2):495-502.
 Konecki D, Kramer G, Pinphanichakarn P, Hardesty B. Polyamines are necessary for maximum in vitro synthesis of globin peptides and play a role in chain initiation. Arch Biochem Biophys. 1975;169(1):192-98.
 Igarashi K, Kojima M, Watanabe Y, Maeda K, Hirose S. Stimulation of polypeptide synthesis by spermidine at the level of initiation in rabbit reticulocyte and wheat germ cell-free systems. Biochem Biophys Res Commun. 1980;97(2):480-6.
 Hunter AR, Farrell PJ, Jackson RJ, Hunt T. The role of polyamines in cell-free protein synthesis in the wheat-germ system. Eur J Biochem. 1977;75(1):149-57.
 Tabor CW, Tabor H. 1,4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem. 1976;45:285-306.
 Wagner EG, Jelenc PC, Ehrenberg M, Kurland CG. Rate of elongation of polyphenylalanine in vitro. Eur J Biochem. 1982;122(1):193-7.
 Vazquez D. Inhibitors of protein biosynthesis. Berlin: SprinВger, 1979: 161-8.
 Uritani M, Miyazaki M. Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts. J Biochem. 1988;103(3):522-30.
 Jim?nez A, Carrasco L, V?zquez D. Enzymic and nonenzymic translocation by yeast polysomes. Site of action of a number of inhibitors. Biochemistry. 1977;16(21):4727-30.