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
- 1 January 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 91 (1) , 291-299
- https://doi.org/10.1093/oxfordjournals.jbchem.a133687
Abstract
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 α-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.Keywords
This publication has 1 reference indexed in Scilit:
- In vitro Synthesis of Bacteriophage LysozymeNature, 1967