[30] Mammalian release factor; in Vitro Assay and Purification☆
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Cited by (37)
Dysfunctions of the translational machinery in digestive glands of mussels exposed to mercury ions
2013, Aquatic ToxicologyCitation Excerpt :When complex eRF1·eRF3·GTP binds to the A-site of such a complex, [3H]Met releases from the ribosome. Therefore, such a system enables the evaluation of the efficiency of the termination process, by monitoring the reduction of radioactivity bound to the ribosome (Caskey et al., 1974). As indicated in Fig. 6A, exposure of mussels to Hg2+ causes a time-dependent reduction in the termination efficiency, which at the 15th day of the exposure reaches the 55% of the control value.
In Vitro Reconstitution of Eukaryotic Translation Reveals Cooperativity between Release Factors eRF1 and eRF3
2006, CellCitation Excerpt :It has been suggested that eRF3 might perform a role similar to that of prokaryotic RF3 by promoting recycling of eRF1 (Zavialov et al., 2001), but recent genetic data suggest that eRF3's GTPase activity might instead couple termination-codon recognition by eRF1 with efficient peptide release (Salas-Marco and Bedwell, 2004). The principal assay used for many years to study termination in vitro is based on artificial pre-TCs obtained by binding an AUG initiation codon and a stop signal (UAAA, UAGA, or UGAA) to “empty” ribosomes reconstituted from 40S and 60S subunits in the presence of [35S]fMet-tRNA to simulate peptidyl tRNA (Caskey et al., 1974). Release of [35S]fMet from fMet-tRNA mimics peptidyl-tRNA hydrolysis.
‘Stop’ in protein synthesis is modulated with exquisite subtlety by an extended RNA translation signal
2018, Biochemical Society TransactionsTwo-step model of stop codon recognition by eukaryotic release factor eRF1
2013, Nucleic Acids Research
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This work was supported by Grant GM-18682-02.