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Nucleic Acids Symposium Series 2005 49(1):307-308; doi:10.1093/nass/49.1.307
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© 2005 Oxford University Press

Molecular recognition of histidine tRNA by histidyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1

Yukari Nagatoyo1, Jun Iwaki1, Satoko Suzuki2, Atsushi Kuno3 and Tsunemi Hasegawa1,2

1 Graduate School of Science and Technology, Yamagata University, Yamagata 990-8560, Japan, 2 Faculty of Science, Yamagata University, Yamagata 990-8560, Japan, 3 National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan

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.


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