title: Molecular recognition of histidine tRNA by histidyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.
abstract: 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.
authors.affiliation: Graduate School of Science and Technology, Yamagata University, Yamagata 990-8560, Japan.
authors.forename: Yukari
authors.initials: Y
authors.lastname: Nagatoyo
authors.forename: Jun
authors.initials: J
authors.lastname: Iwaki
authors.forename: Satoko
authors.initials: S
authors.lastname: Suzuki
authors.forename: Atsushi
authors.initials: A
authors.lastname: Kuno
authors.forename: Tsunemi
authors.initials: T
authors.lastname: Hasegawa
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D012354:RNA, Transfer, His; D006643:Histidine-tRNA Ligase