Molecular recognition of histidine tRNA by histidyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.
To investigate the recognition sites of histidine tRNA for histidyl-tRNA synthetase from an extreme hyperthermophilic archaeon, Aeropyrum pernix K1, we examined histidylation activities by using overexpressed histidyl-tRNA synthetase and various histidine tRNA transcripts that were prepared by in vitro transcription system. Results indicated that anticodon was not recognized by the histidyl-tRNA synthetase similar to that of Escherichia coli histidine tRNA recognition system. Discriminator base C73 was weekly recognized and an additional G residue was specifically recognized by the enzyme.
Nagatoyo
Yukari
Y
Graduate School of Science and Technology, Yamagata University, Yamagata 990-8560, Japan.
Iwaki
Jun
J
Suzuki
Satoko
S
Kuno
Atsushi
A
Hasegawa
Tsunemi
T
D041522:Aeropyrum / Q000201:enzymology*; D019843:Archaeal Proteins / Q000378:metabolism*; D006643:Histidine-tRNA Ligase / Q000378:metabolism*; D012354:RNA, Transfer, His / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D019843:Archaeal Proteins; D012354:RNA, Transfer, His; D006643:Histidine-tRNA Ligase