Protein-directed ribosomal frameshifting temporally regulates gene expression

Sawsan Napthine, Roger Ling, Leanne K. Finch, Joshua D. Jones, Susanne Bell, Ian Brierley () and Andrew E. Firth ()
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Sawsan Napthine: University of Cambridge
Roger Ling: University of Cambridge
Leanne K. Finch: University of Cambridge
Joshua D. Jones: University of Cambridge
Susanne Bell: University of Cambridge
Ian Brierley: University of Cambridge
Andrew E. Firth: University of Cambridge

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Programmed −1 ribosomal frameshifting is a mechanism of gene expression, whereby specific signals within messenger RNAs direct a proportion of translating ribosomes to shift −1 nt and continue translating in the new reading frame. Such frameshifting normally occurs at a set ratio and is utilized in the expression of many viral genes and a number of cellular genes. An open question is whether proteins might function as trans-acting switches to turn frameshifting on or off in response to cellular conditions. Here we show that frameshifting in a model RNA virus, encephalomyocarditis virus, is trans-activated by viral protein 2A. As a result, the frameshifting efficiency increases from 0 to 70% (one of the highest known in a mammalian system) over the course of infection, temporally regulating the expression levels of the viral structural and enzymatic proteins.

Date: 2017
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DOI: 10.1038/ncomms15582

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