Molecular recognition of threonine tRNA by threonyl-tRNA synthetase from an extreme thermophilic archaeon, Aeropyrum pernix K1.
To investigate the recognition sites of tRNA(Thr) for threonyl-tRNA synthetase (ThrRS) from an extreme thermophilic and aerobic archaeon, Aeropyrum pernix K1, threonylation experiments using various in vitro mutant transcripts of tRNA(Thr) were examined. The results indicated that A. pernix ThrRS did recognize the first three base pairs of acceptor stem in addition to the second and the third letters of anticodon of tRNA(Thr), in spite of its N-terminal truncated unique structure. Discriminator base was not involved in recognition by A. pernix ThRS. These determinants were confirmed by the identity switching experiments from the in vitro mutants of A. pernix tRNA(Pro) and tRNA(Asn).
Nagaoka
Yoshiyuki
Y
Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.
Yokozawa
Junji
J
Umehara
Takuya
T
Iwaki
Jun
J
Okamoto
Koji
K
Kawarabayasi
Yutaka
Y
Koyama
Yoshinori
Y
Sako
Yoshihiko
Y
Wakagi
Takayoshi
T
Kuno
Atsushi
A
Hasegawa
Tsunemi
T
D001105:Archaea / Q000201:enzymology*; D012363:RNA, Transfer, Thr / Q000235:genetics / Q000378:metabolism*; D013914:Threonine-tRNA Ligase / Q000378:metabolism*
D012363:RNA, Transfer, Thr; D013914:Threonine-tRNA Ligase