ArticleNucleic acids research2020
An in vitro single-molecule assay for eukaryotic cap-dependent translation initiation kinetics.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The separation between mRNA-ends is more variable than expected.FEBS open bio · 2024Article
- Single-molecule visualization of mRNA circularization during translation.Experimental & molecular medicine · 2023Review
- Translational buffering by ribosome stalling in upstream open reading frames.PLoS genetics · 2022Article
- Smart-ORF: a single-molecule method for accessing ribosome dynamics in both upstream and main open reading frames.Nucleic acids research · 2021Article
- An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics.Journal of visualized experiments : JoVE · 2020Article
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Authors and funding
4 authors.
Funding
Abstract
Eukaryotic mRNAs are predominantly translated via the cap-dependent pathway. Initiation is a rate-limiting step in cap-dependent translation and is the main target of translational control mechanisms. There is a lack of high-resolution techniques for characterizing the cap-dependent initiation kinetics. Here, we report an in vitro single-molecule assay that allows characterization of both initiation and peptide chain elongation kinetics for cap-dependent translation. Surprisingly, the histogram of the first-round initiation time is highly asymmetrical and spans a large time range that is several-fold greater than the average peptide synthesis time in translation reactions with a firefly luciferase-encoding mRNA. Both the histogram and single-molecule trajectories reveal an unexpected high-degree of asynchrony in translation activity between mRNA molecules. Furthermore, by inserting a small stem-loop (ΔG = -4.8 kcal/mol) in the middle of the mRNA 5' untranslated region (UTR), our assay robustly detects small changes in budding yeast initiation kinetics, which could not be resolved by bulk luminescence kinetics. Lastly, we demonstrate the general applicability of this assay to distinct cell-free translation systems by using extracts prepared from budding yeast, wheat germ, and rabbit reticulocyte lysates. This assay should facilitate mechanistic studies of eukaryotic cap-dependent translation initiation and translational control.
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