Determination of tryptophan tRNA recognition sites for tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.
To investigate the recognition mechanism of tryptophan tRNA by tryptophanyl-tRNA synthetase from extreme hyperthermophilic and aerobic archaeon, Aeropyrum pernix K1, tryptophanylation activities were examined by using mutant tryptophan tRNA transcripts prepared by in vitro transcription system. Their transcripts were aminoacylated with tryptophan by overexpressed A. pernix tryptophanyl-tRNA synthetase. The results indicated that anticodon nucleotides C34, C35 and A36, discriminator base A73, G1-C72 and G2-C71 base pairs of acceptor stem were base-specifically recognized by A. pernix tryptophanyl-tRNA synthetase.
Tsuchiya
Wataru
W
Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.
Umehara
Takuya
T
Kuno
Atsushi
A
Hasegawa
Tsunemi
T
D041522:Aeropyrum / Q000201:enzymology*; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism*
D012346:RNA, Transfer, Amino Acyl; D014369:Tryptophan-tRNA Ligase