Protein biosynthesis is a highly accurate biological process essential for life. Amino acid misincorporation errors (mistranslation) normally occur at low levels, but can increase sharply upon amino acid starvation, exposure to drugs, oxidative stress and other physiological perturbations. These processes disrupt protein function and are normally regarded as being deleterious, however, recent work has shown that they can also be regulated to produce advantageous phenotypes in both prokaryotes and eukaryotes. The biology of such unexpected adaptive mistranslation is poorly understood due to technical difficulties in the identification and quantification of amino acid misincorporations. In this mini-review, we describe proteome scale methodologies involving the use of massspectrometry and bioinformatics tools to directly detect and quantify mistranslation events and also indirect functional methods that permit sensitive, flexible and low-cost analysis of site specific amino acid variation.
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