ArticleFrontiers in molecular biosciences2026
Full-protein release assay in a reconstituted yeast translation system using GGQ-methylated eRF1.
Article in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Translation termination in eukaryotes requires the concerted action of release factors eRF1 and eRF3, together with accessory factors including eIF5A and Rli1, to achieve efficient peptide release from the ribosome. Here, we establish a yPURE system-based Termi-nLuc assay, in which pre-termination complexes (PreTCs), carrying full-length nanoluciferase (nLuc) peptidyl-tRNA, are formed by simply omitting release factors from the reconstituted yeast translation system, enabling rapid and sensitive analysis without the need for sucrose density gradient purification. To enable direct biochemical analysis of GGQ methylation-a physiologically important modification of eRF1 whose effects on peptide release activity had not previously been examined
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