J. Biochem, 1982, Vol. 91, No. 1 291-299
© 1982 Japanese Biochemical Society
research-article |
Interaction of Aminoacyl-tRNA with Bacterial Elongation Factor Tu : GTP Complex: Effects of the Amino Group of Amino Acid Esterified to tRNA, the Amino Acid Side Chain, and tRNA Structure
Institute of Molecular Biology, Faculty of Science, Nagoya University Chikusa-ku, Nagoya, Aichi 464
2 To whom correspondence should be addressed
The present investigation was undertaken to see to what extent the a-amino group of the amino acid, the side chain of the amino acid of aminoacyl-tRNA, and th tRNA structure are involved in determining the affinity of aminoacyl-tRNA for bacterial elongation factor Tu-GTP complex. Various aminoacyl-tRNAs, mis aminoacylated tRNAs, and formylated aminoacyl-tRNAs were prepared, and the dissociation constants of the ternary complexes of aminoacyl-tRNA with EF-Tu: GTP were determined by the RNase-resistance assay. The results indicated that the free
-amino group of the amino acids in aminoacyl-tRNA is strongly required for binding with EF-Tu: GTP. In this connection, the biological significance of formylation for Met-tRNAMetf species is discussed.
1 Present address: Laboratory of Biochemical Preparation, Mitsubishi-Kasei Institute of Life Sciences, Minamiooya, Machida, Tokyo 194