A novel reporter for translational recoding by the Foot-and-mouth disease 2A peptide

A novel reporter for translational recoding by the Foot-and-mouth disease 2A peptide
Protein synthesis follows simple rules, ribosomes initiating at a methionine codon, and continuing through the open reading frame to a stop codon, where translation terminates. There are exceptions to this, where proteins that differ from what would be expected by initial examination of mRNA sequence are produced. Examples include ribosomes shifting reading frame or reading through stop codons. Such events are programmed translational recoding. Recoding is frequently found in viral gene expression. A focus of study in the laboratory is a recoding event, the 2A reaction, first found in foot-and-mouth disease virus, but also seen in other viruses. The 2A reaction produces two separate proteins from a single ORF, and is driven by the nascent (2A) peptide chain. When just translated and within the exit tunnel of the ribosome, 2A drives a skip in peptide bond formation between the its final 2 amino acids, glycine and proline. The 2A peptide works when placed within any open reading frame, 'breaking' the corresponding protein into two fragments. We wish to generate and test new genetic reporters of 2A, where we can assess the efficiency of the reaction by readily measured read-out. This will facilitate analysis of factors that affect the efficiency of the reaction. In this project 2A inserted into the gene encoding green fluorescent protein will be tested using yeast as the expression system. Starting constructs have been generated, and the project will focus on characterising them, with the possibility of using them in a genetic screen. 2A is frequently used in Biomedical and Biotechnological applications. Increased understanding of how 2A functions is of importance to optimising its use in these areas. As the 2A reaction is required for some viruses to replicate, it also represents a possible target for antivirals.

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