Biopolym. Cell. 1989; 5(5):5-18.
Огляди
Транспортна РНК як фактор регуляції білкового гомеостазу
1Негруцький Б. С.
  1. Інститут молекулярної біології і генетики АН УСРС
    Київ, СРСР

Abstract

В огляді критично розглянуто експериментальні дані щодо участі тРНК у регуляції білкового синтезу і деградації білків за умов амінокислотного голодування. Передбачається, що тРНК може бути одним з посередників у координованої регуляції цих процесів.

References

[1] Hershko A, Ciechanover A. Mechanisms of intracellular protein breakdown. Annu Rev Biochem. 1982;51:335-64.
[2] Translation regulation of gene expression Ed. J. Ilan. New York: Plenum Press, 1987. 487 P.
[3] Goldberg AL, St John AC. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747-803.
[4] Hamilton TA, Litt M. Biosynthesis of mammalian transfer RNA. Evidence for regulation by deacylated transfer RNA. Biochim Biophys Acta. 1976;435(4):362-75.
[5] Grummt F, Grummt I. Studies on the role of uncharged tRNA in pleiotypic response of animal cells. Eur J Biochem. 1976;64(1):307-12.
[6] Arfin SM, Simpson DR, Chiang CS, Andrulis IL, Hatfield GW. A role for asparaginyl-tRNA in the regulation of asparagine synthetase in a mammalian cell line. Proc Natl Acad Sci U S A. 1977;74(6):2367-9.
[7] Flaim KE, Peavy DE, Everson WV, Jefferson LS. The role of amino acids in the regulation of protein synthesis in perfused rat liver. I. Reduction in rates of synthesis resulting from amino acid deprivation and recovery during flow-through perfusion. J Biol Chem. 1982;257(6):2932-8.
[8] van Venrooij WJ, Henshaw EC, Hirsch CA. Effects of deprival of glucose or individual amino acids on polyribosome distribution and rate of protein synthesis in cultured mammalian cells. Biochim Biophys Acta. 1972;259(1):127-37.
[9] Mader A. A transcription-translation activation feedback circuit as a function of protein degradation, with the quality of protein mass adaptation related to the average functional load. J Theor Biol. 1988;134(2):135-57.
[10] Kisselev LL, Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 P.
[11] Osterman LA. Participation of tRNA in regulation of protein biosynthesis at the translational level in eukaryotes. Biochimie. 1979;61(3):323-42.
[12] Ciechanover A. Regulation of the ubiquitin-mediated proteolytic pathway: role of the substrate alpha-NH2 group and of transfer RNA. J Cell Biochem. 1987;34(2):81-100.
[13] El'skaia AV, Matsuka GKh. Contribution to alteration in the composition of individual t-RNAs in mammary gland cells depending on the quality of the synthesized proteins. Ukr Biokhim Zh. 1968;40(2):120-5.
[14] Hentzen D, Chevallier A, Garel JP. Differential usage of iso-accepting tRNASer species in silk glands of Bombyx mori. Nature. 1981;290(5803):267-9.
[15] Smith DW, McNamara AL. The distribution of transfer ribonucleic acid in rabbit reticulocytes. Levels of aminoacylation and ribosomal attachment during hemoglobin synthesis. J Biol Chem. 1974;249(5):1330-4.
[16] Garel JP. Functional adaptation of tRNA population. J Theor Biol. 1974;43(1):211-25.
[17] Shakulov RS, Klyachko EV. Non-translated function of ribosomes. Itogi nauki I tekhniki. Moscow, VINITI, 1983; 194-237 (Ser. Biol. Khimiya; Vol. 18).
[18] Smulson M. Amino acid deprivation of human cells: effects on RNA synthesis, RNA polymerase, and ribonucleoside phosphorylation. Biochim Biophys Acta. 1970;199(2):537-40.
[19] Mamont P, Hershko A, Kram R, Schacter L, Lust J, Tomkins GM. The pleiotypic response in mammalian cells: search for an intracellular mediator. Biochem Biophys Res Commun. 1972;48(6):1378-84.
[20] von Heijne G, Blomberg C, Liljenstrom H. Theoretical modelling of protein synthesis. J Theor Biol. 1987;125(1):1-14.
[21] Austin SA, Pain VM, Lewis JA, Clemens MJ. Investigation of the role of uncharged tRNA in the regulation of polypeptide chain initiation by amino acid starvation in cultured mammalian cells; a reappraisal. Eur J Biochem. 1982;122(3):519-26.
[22] Pain VM, Henshaw EC. Initiation of protein synthesis in Ehrlich ascites tumour cells. Evidence for physiological variation in the association of methionyl-tRNAf with native 40-S ribosomal subunits in vivo. Eur J Biochem. 1975;57(2):335-42.
[23] Ogilvie A, Huschka U, Kersten W. Control of protein synthesis in mammalian cells by aminoacylation of transfer ribonucleic acid. Biochim Biophys Acta. 1979;565(2):293-304.
[24] Flaim KE, Liao WS, Peavy DE, Taylor JM, Jefferson LS. The role of amino acids in the regulation of protein synthesis in perfused rat liver. II. Effects of amino acid deficiency on peptide chain initiation, polysomal aggregation, and distribution of albumin mRNA. J Biol Chem. 1982;257(6):2939-46.
[25] Shenoy ST, Rogers QR. Effect of starvation on the charging levels of transfer ribonucleic acid and total acceptor capacity in rat liver. Biochim Biophys Acta. 1977;476(3):218-27.
[26] McNurlan MA, Tomkins AM, Garlick PJ. The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochem J. 1979;178(2):373-9.
[27] Sato A, Noda K, Natori Y. The effect of protein depletion on the rate of protein synthesis in rat liver. Biochim Biophys Acta. 1979;561(2):475-83.
[28] Balkow K, Rabinovitz M. Increased binding of transfer ribonucleic acid species to ribosomes under conditions interfering with their aminoacylation. Mol Pharmacol. 1973;9(2):229-36.
[29] Hansen BS, Vaughan MH, Wang L. Reversible inhibition by histidinol of protein synthesis in human cells at the activation of histidine. J Biol Chem. 1972;247(12):3854-7.
[30] Vaughan MH, Hansen BS. Control of initiation of protein synthesis in human cells. Evidence for a role of uncharged transfer ribonucleic acid. J Biol Chem. 1973;248(20):7087-96.
[31] Arnstein HR, Barwick CW, Lange JD, Thomas HD. Control of protein synthesis by amino acid supply. The effect of asparagine deprivation on the translation of messenger RNA in reticulocyte lysates. FEBS Lett. 1986;194(1):146-50.
[32] Aspen AJ, Hoagland MB. Uncoupling of amino acid turnover on transfer RNA from protein synthesis in HeLa cells. Biochim Biophys Acta. 1978;518(3):482-96.
[33] Allen RE, Raines PL, Regen DM. Regulatory significance of transfer RNA charging levels. I. Measurements of charging levels in livers of chow-fed rats, fasting rats, and rats fed balanced or imbalanced mixtures of amino acids. Biochim Biophys Acta. 1969;190(2):323-36.
[34] Sox HC Jr, Hoagland MB. Functional alterations in rat liver polysomes associated with starvation and refeeding. J Mol Biol. 1966;20(1):113-21.
[35] Lee SY, Krsmanovic V, Brawerman G. Initiation of polysome formation in mouse sarcoma 180 ascites cells. Utilization of cytoplasmic messenger ribonucleic acid. Biochemistry. 1971;10(5):895-900.
[36] Zasloff M. Non-enzymic binding of formylmethionyl-transfer RNAf to Artemia salina ribosomes. J Mol Biol. 1973;76(4):445-53.
[37] Kyner D, Zabos P, Levin DH. Inhibition of protein chain initiation in eukaryotes by deacylated transfer RNA and its reversibility by spermine. Biochim Biophys Acta. 1973;324(3):386-96.
[38] Austin SA. Effect of histidinol on the initiation and elongation of protein synthesis in Krebs II ascites cells. Biochem Soc Trans. 1976;4(4):781-3.
[39] Jakubowicz T, Frielle DW, Vaughan MH. 40S subunit X Met-tRNAf complexes and initiation factor eIF-2 phosphorylation in mammalian cells accumulating uncharged tRNA. Acta Biochim Pol. 1985;32(3):199-210.
[40] Poso AR, Wert JJ Jr, Mortimore GE. Multifunctional control of amino acids of deprivation-induced proteolysis in liver. Role of leucine. J Biol Chem. 1982;257(20):12114-20.
[41] Poso AR, Mortimore GE. Requirement for alanine in the amino acid control of deprivation-induced protein degradation in liver. Proc Natl Acad Sci U S A. 1984;81(14):4270-4.
[42] Mortimore GE. Mechanisms of Cellular Protein Catabolism. Nutrition Reviews. 2009;40(1):1-12.
[43] Scornik OA. Faster protein degradation in response to decreases steady state levels of amino acylation of tRNAHis in Chinese hamster ovary cells. J Biol Chem. 1983;258(2):882-6.
[44] Ovcharenko GV, Babii TP, Matsuka GKh. The effect of fasting on the aminoacyl-tRNA content in the rabbit liver. Ukr Biokhim Zh. 1971;43(6):708-11.
[45] Matsuka GKh, Skvirskaia EB, Babii TP, Baturina ID, Pozdniakova TM, Khomenko AK. Acceptor activity of transfer RNA during starvation. Ukr Biokhim Zh. 1968;40(2):115-9.
[46] Matsuka GKh, Babii TP, Skvirskaia EB, Kovalenko MI. Changes in the ability of t-RNA of rabbit liver to accept amino acids during fasting. Ukr Biokhim Zh. 1969;41(6):655-9.
[47] Matsuka GKh, Babii TP, Skvirskaia EB, Kovalenko MI, Semenikhin VI. Possibility of existence in animal tissues of different conformation forms of t-RNA, differing by ability to accept amino acids. Ukr Biokhim Zh. 1970;42(1):24-7.
[48] Lindahl T, Adams A, Fresco JR. Renaturation of transfer ribonucleic acids through site binding of magnesium. Proc Natl Acad Sci U S A. 1966;55(4):941-8.
[49] Gartland WJ, Sueoka N. Two interconvertible forms of tryptophanyl sRNA in E. coli. Proc Natl Acad Sci U S A. 1966;55(4):948-56.
[50] Kearns DR, Wong YP, Hawkins E, Chang SH. Model for the secondary structure of the denaturated conformer of yeast tRNA3Leu. Nature. 1974;247(5442):541-3.
[51] Jones CR, Kearns DR. Nuclear magnetic resonance of the base-pairing structure of the native and denatured conformers of Escherichia coli transfer RNATrp. J Mol Biol. 1976;103(4):747-64.
[52] Bina-Stein M, Crothers DM, Hilbers CW, Shulman RG. Physical studies of denatured tRNA2Glu from Escherichia coli. Proc Natl Acad Sci U S A. 1976;73(7):2216-20.
[53] Matsuka GKh, Babii TP, Skvirskaia EB, Ovcharenko GV, Semenikhin VI. Biologically inactive transfer RNA in animal livers. Biokhimiia. 1973;38(6):1221-7.
[54] Transfer ribonucleic acid. Some aspects of structure and function. Ed. GKh Matsuka. Kiev, Naukova Dumka, 1976; 220 P.
[55] Tamulyavichius AI. Functional characterization of transfer ribonucleic acids and aminoacyl-tRNA synthetases in myocardial ischemia: Author. dis. ... Kand. biol. nauk. Vilnius, 1985. 18p.
[56] El'skaya A, Negrutskii B. The interaction between biologically inactive tRNA conformers and leucyl-tRNA synthetase from rabbit liver. Eur J Biochem. 1987;164(1):65-9.
[57] Negrutsky BS, Elskaya AV. The interaction of different conformers of deacylated tRNA with 80S ribosomes. Biopolym. Cell. 1987; 3(3):131-4.
[58] Negrutskii BS, El'skaia AV. Influence of various tRNA conformers on mRNA translation in cell-free protein-synthesizing systems. Ukr Biokhim Zh. 1989;61(3):58-62.
[59] Harley CB, Pollard JW, Stanners CP, Goldstein S. Model for messenger RNA translation during amino acid starvation applied to the calculation of protein synthetic error rates. J Biol Chem. 1981;256(21):10786-94.
[60] Potapov AP, Elskaya AV. Natural mRNA translation. I. General kinetic analysis of the process of one mRNA species translation. Biopolym. Cell. 1986; 2(2):88-92.
[61] Pelletier J, Sonenberg N. The involvement of mRNA secondary structure in protein synthesis. Biochem Cell Biol. 1987;65(6):576-81.
[62] Rodnina MV, Negrutskii BS. Deacylated tRNA and control of translation. Structure and function of bioPolymers: Proc. of rePorts ResP. conf. (Lviv, 1989). Kiev, 1989; 54.
[63] Wintermeyer W, Lill R, Paulsen H, Robertson JM. Mechanism of Ribosomal Translocation. Structure, function and genetics of ribosomes Eds B. Hardesty G. Kramer. New York: Springer, 1986:523-540. ttp://
[64] Kirillov SV, Semenkov YuP. Extension of Watson's model for the elongation cycle of protein biosynthesis. J Biomol Struct Dyn. 1986;4(2):263-9.
[65] Robertson JM, Wintermeyer W. Mechanism of ribosomal translocation. tRNA binds transiently to an exit site before leaving the ribosome during translocation. J Mol Biol. 1987;196(3):525-40.
[66] Graf H. Intraction of aminoacyl-tRNA synthetases with ribosomes and ribosomal subunits. Biochim Biophys Acta. 1976;425(2):175-84.
[67] Rechsteiner M. Ubiquitin-mediated pathways for intracellular proteolysis. Annu Rev Cell Biol. 1987;3:1-30.
[68] Scornik OA, Ledbetter ML, Malter JS. Role of aminoacylation of histidyl-tRNA in the regulation of protein degradation in Chinese hamster ovary cells. J Biol Chem. 1980;255(13):6322-9.
[69] Ciechanover A, Wolin SL, Steitz JA, Lodish HF. Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system. Proc Natl Acad Sci U S A. 1985;82(5):1341-5.
[70] Ferber S, Ciechanover A. Transfer RNA is required for conjugation of ubiquitin to selective substrates of the ubiquitin- and ATP-dependent proteolytic system. J Biol Chem. 1986;261(7):3128-34.
[71] Liljenstrom H. Maintenance of accuracy during amino acid starvation. FEBS Lett. 1987;223(1):1-5.