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The structure of histidine tRNA (tRNA) is different from tRNA structures of other amino acids specificities by the presence of an extra nucleotide on the 5’-end (G-1). To study the molecular mechanism of interaction of tRNA with histidyl-tRNA synthetase the purification method of T.thermophilus tRNA was elaborated and the primary structure of isoacceptor form of tRNA 1 His was studied. Individual tRNA was isolated from the crude tRNA, using the combination of low pressure chromatography on benzoyl-DEAE-cellulose (BD-cellulose) and DEAE Toyopearl 650 with high pressure liquid chromatography on DEAE 5PW and Ultrapore C8 columns. The primary structure of T.thermophilus tRNA 1 His was determined using the method of rapid gel-sequencing. The studied structure is different from Escherichia coli tRNA in 23 positions. The interaction sites of T.thermophilus tRNA with histidyl-tRNA synthetase were investigated using the method of chemical modification by ethylnitrosourea. It was shown that histidyl-tRNA synthetase protects the following phosphates of tRNA from alkylation by ethylnitrosourea: 8 – between acceptor and D-stem; 27, 28, 29 – from 5’-side of anticodon stem; phosphate 34 in anticodon and phosphates 67, 68 from 3’-side of acceptor stem. All the revealed sites of tRNA are localized on one side of three-dimensional structure of tRNA in the same one where the variable stem side is. D-stem is located on the opposite side and does not interact with the enzyme.

biopolymers and cell

The isolation of histidine tRNA from Thermus thermophilus and the study of its primary structure and interaction sites with homologous aminoacyl-tRNA synthetase