Abstract

The genetic code expansion strategy has become an elegant method for site-specific incorporation of noncanonical amino acids with diverse functionalities into proteins of interest in bacteria, yeast, mammalian cells, and even animals. This technique allows precise labeling as well as manipulation of a given protein to dissect its physiological and/or pathological roles under living conditions. Here, we demonstrate the extension of a recently emerged pyrrolysine-based genetic code expansion strategy for encoding noncanonical amino acids into enteric bacterial pathogens.

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