Recognition of tRNA by aminoacyl-tRNA synthetase from hyperthermophilic archaea, Aeropyrum pernix K1.
To study the recognition sites of tRNA for archaeal aminoacyl-tRNA synthetase, several aminoacyl-tRNA synthetase genes from hyperthermophilic archaeon, Aeropyrum pernix K1 were cloned and expressed. All the expressed enzymes showed extreme thermostability. Expressed threonyl-tRNA synthetase threonylated not only archaeal (A. pernix and Haloferax volcanii) threonine tRNAs but also Escherichia coli threonine tRNA. However, threonyl-tRNA synthetase from H. volcanii did not threonylate E. coli threonine tRNA.
Yokozawa
J
J
Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.
Nagaoka
Y
Y
Umehara
T
T
Iwaki
J
J
Kawarabayasi
Y
Y
Koyama
Y
Y
Sako
Y
Y
Wakagi
T
T
Kuno
A
A
Hasegawa
T
T
D019620:Desulfurococcaceae / Q000201:enzymology*; D004795:Enzyme Stability; D006358:Hot Temperature; D019642:RNA, Archaeal / Q000378:metabolism; D012329:RNA, Bacterial / Q000378:metabolism; D012363:RNA, Transfer, Thr / Q000378:metabolism*; D013379:Substrate Specificity; D013914:Threonine-tRNA Ligase / Q000378:metabolism*
D019642:RNA, Archaeal; D012329:RNA, Bacterial; D012363:RNA, Transfer, Thr; D013914:Threonine-tRNA Ligase