J Mol Biol. 2012 Mar 2;416(4):465-6.
Commentary on Vendeix et al. J Mol Biol. 2012
Alfonzo, JD.
Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
For many years, the laboratories of Agris et al.6 and others [7], [8], [9] and [10] have painstakingly shown that modifications play key roles in codon binding and can even have a direct bearing as aminoacylation determinants. However, difficulty with chemical synthesis has remained a barrier to defining the individual contributions of modifications to tRNAUUULys3 function. Vendeix et al. have now devised a protocol that allows the simultaneous quantitative and stoichiometrically correct synthesis of either a fully modified tRNALys ASL or variants missing one or more of the modifications.
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