The conformation change of Thermus thermophilus tRNAIle1 upon complex formation with T. thermophilus elongation factor Tu (EF-Tu) was studied by analysis of the circular dichroism (CD) bands at 315 nm (due to the 2-thioribothymidine residue in the T-loop) and at 295 nm (due to the core structure of tRNA). Formation of the ternary complex of isoleucyl-tRNAIle1 and EF-Tu·GTP increased the intensities of these CD bands, indicating stabilization of the association between the T-loop and the D-loop and also a significant conformation change of the core region. Upon complex formation of EF-Tu·GTP and unchanged tRNA, however, the conformation of the core region is not changed, while the association of the two loops is still stabilized. On the other hand, the binding with EF-Tu·GDP does not appreciably affect the conformation of isoleucyl-tRNA or unchanged tRNA. These indicate the importance of the γ-phosphate group of GTP and the aminoacyl group in the formation of the active complex of aminoacyl-tRNA and EF-Tu·GTP. © 1990.
Haruki, M., Matsumoto, R., Hara-Yokoyama, M., Miyazawa, T., & Yokoyama, S. (1990). Conformational changes of aminoacyl-tRNA and unchanged tRNA upon complex formation with polypeptide chain elongation factor Tu. FEBS Letters, 263(2), 361–364. https://doi.org/10.1016/0014-5793(90)81414-J