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Summary
By controlling gene expression at the level of translation, cells can fine-tune protein abundance, respond quickly to environmental changes, and restrict synthesized proteins to specific places within the cell. Whereas the basic biochemistry of translation is understood in great detail, questions remain about translation in the context of the cell: how ribosomes load onto a messenger RNA (mRNA), how fast and how far translating ribosomes move, and how rapidly translation reacts to the environment. On pages 1425 and 1430 of this issue, studies by Morisaki et al. (1) and Wu et al. (2), respectively, as well as papers in Cell by Yan et al. (3) and Wang et al. (4), provide a new view of translation by developing real-time imaging of nascent peptides being synthesized from single mRNAs in cells. These novel technologies provided versatile frameworks for quantitative in vivo translation studies and revealed hidden aspects of proteins synthesis.
