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Threonyl-tRNA synthetase of archaea: Importance of the discriminator base in the aminoacylation of threonine tRNA
Author(s) -
Hisayuki Ishikura,
Yoshiyuki Nagaoka,
Junji Yokozawa,
Tadashi Umehara,
Atsushi Kuno,
Taro Hasegawa
Publication year - 2000
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/44.1.83
Subject(s) - aminoacylation , haloferax volcanii , transfer rna , threonine , escherichia coli , biology , biochemistry , archaea , base pair , serine , enzyme , rna , dna , gene
To investigate the contribution of the discriminator base of archaeal tRNA(Thr) in aminoacylation by threonyl-tRNA synthetase (ThrRS), cross-species aminoacylation between Escherichia coli and Haloferax volcanii, halophilic archaea, was studied. It was found that E. coli ThrRS threonylated the H. volcanii tRNA(Thr) but that E. coli threonine tRNA was not aminoacylated by H. volcanii ThrRS. Results of a threonylation experiment using in vitro mutants of E. coli threonine tRNA showed that only the mutant tRNA(Thr) having U73 was threonylated by H. volcanii ThrRS. These findings indicate that the discriminator base U73 of H. volcanii tRNA(Thr) is a strong determinant for the recognition by ThrRS.

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