[Comparative analysis of interaction sites of Thermus thermophilus and Escherichia coli tRNA(Tyr) with homologous aminoacyl-tRNA synthetases by means of chemical modification and nuclease hydrolysis].
A nucleotide sequence of tRNA(Tyr) from the extreme thermophile Thermus thermophilus HB-27 living at 75 degrees C was determined. It is 86 nt long and shares a 52% homology with tRNA(Tyr) from Escherichia coli. A comparative analysis of the interaction sites of tRNA(Tyr) from T. thermophilus and E. coli with the cognate aminoacyl-tRNA synthetases was accomplished by the chemical modification and nuclease hydrolysis approaches. The tRNA(Tyr) was shown to interact with the cognate enzyme in the anticodon stem (on the 5'-side), in the anticodon, in the variable stem and loop (on the 5'-side), and in the acceptor stem (on the 3'-side). These regions are located in the variable stem of the L-form. It was demonstrated that, upon forming the complex E. coli tRNA(Tyr)-cognate synthetase, endonuclease V1 induces additional cleavages of phosphodiester bonds on the 3'-side of the anticodon stem and on the 5'-side of the T-stem. This implies that tRNA may change its conformation when it interacts with the enzyme.
Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kiev, Ukraine.
S P
SP
Egorova
A D
AD
Iaremchuk
I A
IA
Kriklivyĭ
M A
MA
Tukalo
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry*; D001345:Autoradiography; D001483:Base Sequence; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics; D006868:Hydrolysis; D008969:Molecular Sequence Data; D012329:RNA, Bacterial / Q000737:chemistry*; D012365:RNA, Transfer, Tyr / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics
D012329:RNA, Bacterial; D012365:RNA, Transfer, Tyr; D012260:Ribonucleases; D000604:Amino Acyl-tRNA Synthetases
Sravnitel'nyĭ analiz uchastkov vzaimodeĭstviia tRNK(Tyr) iz Thermus thermophilus i Escherichia coli s gomologichnymi aminoatsil-tRNK-sintetazami metodami khimicheskoĭ modifikatsii i nukleaznogo gidroliza.