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J. Biol. Chem., Vol. 258, Issue 17, 10360-10365, Sep, 1983
WP Tate, H Hornig and R Luhrmann
Recognition of the termination codon by release factor was studied with 70
S ribosomes containing initiator tRNA at the P site and an amino
acid-specifying codon as well as the corresponding cognate tRNA at the A
site. In vitro termination was not excluded when either the A site was
occupied with an amino acid-specifying codon or the termination codon was
displaced from the A site codon position by spacer nucleotides between UAA
and the P site bound AUG. The release factor may have flexibility in its
codon recognizing domain to be able to adjust to this enforced change in
the position of the termination codon on the ribosome without loss of
functional specificity. Deacylated tRNA bound at the A site of 70 S
ribosomes did not interfere with stoichiometric UAA-directed release factor
binding to these particles. In contrast, a ternary complex (aminoacyl-tRNA
elongation factor-Tu . GTP) abolished the binding of the release factor
while aminoacyl-tRNA inhibited it only weakly. This suggests that release
factor and elongation factor-Tu have overlapping binding sites but the A
site binding domains of the release factor and tRNA are exclusive.
Recognition of termination codon by release factor in the presence of a tRNA-occupied A site. Evidence for flexibility in accommodation of the release factor on the ribosome
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