立体構造からみたグルタミルtRNA合成酵素の進化

概要

論文の詳細を見る
Aminoacyl-tRNA synthetases (aaRS's) play key roles in the correct protein biosynthesis through strict recognition/ligation of the cognate amino acid and tRNA. Our recent study on the crystal structure of glutamyl-tRNA synthetase (GluRS) revealed that GluRS and glutaminyl-tRNA synthetase (GlnRS) share geometrically similar NH_2-terminal half, comprising the class I-specific Rossmann-fold domain and the intervening subclass-specific α/β domain. In striking contrast to the β-barrel structure of the GlnRS COOH-terminal half, the GlnRS COOH-terminal half displays an all-α-helix architecture, an "α-helix cage". Precise alignment of primary structures of GluRSs and GlnRSs on the basis of the tertiary structures indicates that the gene of GlnRS diverged from that of GlnRS in eukaryote, and was transferred laterally from eukaryote to prokaryote ("horizontal gene transfer") in the evolutionary process.
日本生物物理学会の論文
1997-01-25