Bianco, A., et al. Nat. Chem. Biol. 8, 748–750 (2012).

Genetic code expansion methods allow unnatural amino acids carrying useful labels such as fluorophores, cross-linkers or reactive chemical handles to be site-specifically incorporated into proteins in cells and organisms. To date, approaches have been developed for Escherichia coli, yeast, mammalian cells and even Caenorhabditis elegans. Bianco et al. now describe an amber suppressor aminoacyl-tRNA synthetase/tRNACUA pair that allows site-specific unnatural amino acid incorporation into proteins in Drosophila melanogaster. They showed that the approach worked efficiently in both fly embryos and adult flies, in various tissues and even in a subset of cells within a tissue. The approach should facilitate experiments to probe protein function in the fly such as studying signaling kinetics or mapping transient protein interactions.