Biopolym. Cell. 2003; 19(2):151-156.
Structure and Function of Biopolymers
Participation of nitrogen bases in the tertiary folding of tRNALeu from Thermus thermophilus
1Kovalenko O. P., 1Kriklivyi I. A., 1Tukalo M. A.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Reactivity of bases in tRNALeu from T. thermophilus has been studied by chemical modification methods. Obtained results suggest that molecules of tRNALeu have a canonical L-form in solution. Triple interactions (8–14)-21, (13–22)-9 and (15–48)-20a arc observed in the core. The latter two interactions represent the characteristic feature of the class II tRNA tertiary structures. Different reactivity of bases 15 and 21 in tRNALeu and tRNASer from T. thermophilus indicates differences in the core tertiary structure of these tRNAs.

References

[1] Himeno H, Hasegawa T, Ueda T, Watanabe K, Shimizu M. Conversion of aminoacylation specificity from tRNA(Tyr) to tRNA(Ser) in vitro. Nucleic Acids Res. 1990;18(23):6815-9.
[2] Asahara H, Himeno H, Tamura K, Hasegawa T, Watanabe K, Shimizu M. Recognition nucleotides of Escherichia coli tRNA(Leu) and its elements facilitating discrimination from tRNASer and tRNA(Tyr). J Mol Biol. 1993;231(2):219-29.
[3] Asahara H, Himeno H, Tamura K, Nameki N, Hasegawa T, Shimizu M. Escherichia coli seryl-tRNA synthetase recognizes tRNA(Ser) by its characteristic tertiary structure. J Mol Biol. 1994;236(3):738-48.
[4] Tocchini-Valentini G, Saks ME, Abelson J. tRNA leucine identity and recognition sets. J Mol Biol. 2000;298(5):779-93.
[5] Normanly J, Ogden RC, Horvath SJ, Abelson J. Changing the identity of a transfer RNA. Nature. 1986 May 15-21;321(6067):213-9.
[6] Gieg? R, Sissler M, Florentz C. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res. 1998;26(22):5017-35.
[7] Tamura K, Asahara H, Himeno H, Hasegawa T, Shimizu M. Identity elements of Escherichia coli tRNA(Ala). J Mol Recognit. 1991;4(4):129-32.
[8] Biou V, Yaremchuk A, Tukalo M, Cusack S. The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science. 1994;263(5152):1404-10.
[9] Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S. Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J. 2002;21(14):3829-40.
[10] Asahara H, Nameki N, Hasegawa T. In vitro selection of RNAs aminoacylated by Escherichia coli leucyl-tRNA synthetase. J Mol Biol. 1998;283(3):605-18.
[11] Kovalenko OP, Petrushenko ZM, Kriklivy? IA, Iaremchuk AD, Tukalo MA. Comparative study of the reactability of phosphoric acid residues in tRNA(Ser) and tRNA(Leu) from Thermus thermophilus. Bioorg Khim. 1999;25(10):768-73.
[12] Kovalenko OP, Kriklivyi IA, Tukalo MA. Study of tertiary structure elements of tRNASer from Thermus thermophilus in solution. Biopolym Cell. 2000; 16(2):115-23.
[13] Petrushenko ZM, Kovalenko OP, Malchenko NN, Krikliviy IA, Yaremchuk AD, Tukalo MA. The primary structure of tRNASer from Thermus thermophilus. Biopolym Cell. 1997; 13(3):202-8.
[14] Silberklang M, Gillum AM, RajBhandary UL. The use of nuclease P1 in sequence analysis of end group labeled RNA. Nucleic Acids Res. 1977;4(12):4091-108.
[15] Romby P, Moras D, Dumas P, Ebel JP, Gieg? R. Comparison of the tertiary structure of yeast tRNA(Asp) and tRNA(Phe) in solution. Chemical modification study of the bases. J Mol Biol. 1987;195(1):193-204.
[16] Kim SH, Quigley GJ, Suddath FL, McPherson A, Sneden D, Kim JJ, Weinzierl J, Rich A. Three-dimensional structure of yeast phenylalanine transfer RNA: folding of the polynucleotide chain. Science. 1973;179(4070):285-8.
[17] Jack A, Ladner JE, Klug A. Crystallographic refinement of yeast phenylalanine transfer RNA at 2-5A resolution. J Mol Biol. 1976;108(4):619-49.
[18] Romby P, Carbon P, Westhof E, Ehresmann C, Ebel JP, Ehresmann B, Gieg? R. Importance of conserved residues for the conformation of the T-loop in tRNAs. J Biomol Struct Dyn. 1987;5(3):669-87.
[19] Dock-Bregeon AC, Westhof E, Gieg? R, Moras D. Solution structure of a tRNA with a large variable region: yeast tRNASer. J Mol Biol. 1989;206(4):707-22.
[20] Teter M, Quigley GJ, Rich A. The binding of metals to tRNA. Metal ions in genetic information transfer. Eds L. Gunther, L. Eichhorn, G. L. Marzilli. New York: Elsevier, 1981: 233-72.
[21] Westhof E, Dumas P, Moras D. Crystallographic refinement of yeast aspartic acid transfer RNA. J Mol Biol. 1985;184(1):119-45.
[22] Petrushenko ZM, Tukalo MA, Matsuka GKh. A study of the conformation of tRNA(IAGLeu) from the cow mammary gland using chemical modification methods. Bioorg Khim. 1988;14(1):31-6.