Extended Data Fig. 5: eIF5-Cy5.5 functions analogously to its unlabeled version.
From: eIF1 and eIF5 dynamically control translation start site fidelity
(a) Example single-molecule fluorescence data from an experiment that monitored loading of the 43S initiation complex as signaled by 40S-Cy3 (green) in the presence of 40 nM eIF5B-Cy3.5 (orange), and 60S-Cy5 (red). In this experiment, unlabeled eIF1 and eIF5 were present at 290 nM each. (b-d) Cumulative probability plot of the eIF5B binding time, 60S subunit joining time, and the lifetime of eIF5B on the 80S initiation complex. The eIF5B binding time was measured relative to initial loading of the 43S initiation complex, which was signified by either appearance of tRNAi-Cy3 signal (this study) or initial appearance of 40S-Cy3 signal22. The overlapped plots indicate that labeled tRNAi-Cy3 and eIF5-Cy5.5 function analogously as their unlabeled versions.
