Song, H. et al. The crystal structure of human eukaryotic release factor eRF1 mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.
Song, H. et al. The crystal structure of human eukaryotic release factor eRF1 mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.
The 2-thio group is required for the efficient codon recognition, and in the case of mt-tRNAGlu, it is necessary for the recognition by the glutaminyl-tRNA synthetase (17).
This domain is not essential for the function of RFs in stop codon recognition and peptidyl hydrolysis [ 13].
Cheng, Z. et al. Structural insights into eRF3 and stop codon recognition by eRF1.
These structures have, in conjunction with molecular dynamics simulations (Sund et al., 2010), contributed to present-day understanding of the principles of stop codon recognition by class-1 RFs and of their activation of the peptidyl transfer center for hydrolysis of the ester bond in peptidyl-tRNA.
We attempted to recruit UAG for an amino acid in JX1.0, so as to mimic a possible code evolution pathway implicated by RF constriction in stop codon recognition in Tetrahymena, Euplotes, and other eukaryotes.
Start site codon recognition triggers GTP hydrolysis and phosphate release, which is followed by release of eIF2 from the 40S subunit, allowing binding of the 60S ribosomal subunit to join.
Yokoyama, S. et al. Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon.
Furthermore, tRNA met -independent initRNA met -independentrved initiationtion-competent extracts prepared from S. cerevisiae in the presence of edeine, a compound that has been showasto interfere with stalsocobservedogninion by ribosomal subunits carrying ternary complexes.
