Studies of interaction sites between tRNA2Ser from Thermus thermophilus and seryl-tRNA synthetase by chemical modification
DOI:
https://doi.org/10.7124/bc.00048EAbstract
The reaction activity of phosphates of tRNA2Ser from T. thermophilus complexed with it a cognate aminoacyi-tRNA syntlmtase has been defined. Seryl-tRNA synthelase protects phosphates of acceptor, variable, T-stems and T-loop from alkylation by ethyl-nitrosourea.References
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.
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.
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.
Petrushenko ZM, Tukalo MA, Gudzera OI, Rozhko OT, Matsuka GKh. [Determination of interacting segments of tRNA(Leu) from cow mammary glands with homologous aminoacyl-tRNA-synthetase by a chemical modification method]. Bioorg Khim. 1990;16(12):1647-52.
Dietrich A, Romby P, Mar?chal-Drouard L, Guillemaut P, Giegé R. Solution conformation of several free tRNALeu species from bean, yeast and Escherichia coli and interaction of these tRNAs with bean cytoplasmic Leucyl-tRNA synthetase. A phosphate alkylation study with ethylnitrosourea. Nucleic Acids Res. 1990;18(9):2589-97.
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.
Normanly J, Abelson J. tRNA identity. Annu Rev Biochem. 1989;58:1029-49.
Saks ME, Sampson JR, Abelson JN. The transfer RNA identity problem: a search for rules. Science. 1994;263(5144):191-7.
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.
Cusack S, Yaremchuk A, Tukalo M. The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site. EMBO J. 1996;15(11):2834-42.
Schatz D, Leberman R, Eckstein F. Interaction of Escherichia coli tRNA(Ser) with its cognate aminoacyl-tRNA synthetase as determined by footprinting with phosphorothioate-containing tRNA transcripts. Proc Natl Acad Sci U S A. 1991;88(14):6132-6.
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.
Yaremchuk AD, Tukalo MA, Konovalenko AV, Egorova SP, Matsuka GKh. Isolation of seryl-tRNA synthetase from Thermus thermophilus HB-27. Biopolym Cell. 1989; 5(5):83-86.
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.
Veknestern TB. The primary structure of transfer ribonucleic acids. M.: Nauka, 1970: 258.
Vlassov VV, Giegé R, Ebel JP. Tertiary structure of tRNAs in solution monitored by phosphodiester modification with ethylnitrosourea. Eur J Biochem. 1981;119(1):51-9.
Dock-Bregeon AC, Westhof E, Giegé R, Moras D. Solution structure of a tRNA with a large variable region: yeast tRNASer. J Mol Biol. 1989;206(4):707-22.
Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution. J Mol Biol. 1993;234(1):222-33.
Borel F, Vincent C, Leberman R, H?rtlein M. Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity. Nucleic Acids Res. 1994;22(15):2963-9.
