Expansion of the amino acid repertoire in protein biosynthesis of the domesticated silkworm, Bombyx mori

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Mutants of phenylalanyl-tRNA synthetase derived from the domesticated silkworm, Bombyx mori, recognizing phenylalanine(Phe) analogues(unnatural amino acids) as a substrate were generated by introducing point mutations into its amino acid binding pocket. The recognition capacity of the mutants toward several Phe analogues was elucidated in vitro, and the incorporation of Cl-Phe, one of Phe analogues, into protein biosynthesis in the cultured cells of B. mori overexpressing a PheRS mutant was verified. Moreover, a gene encoding methionyl-tRNA synthetase(MetRS) was cloned from B. mori and its complete cDNA sequence was clarified, and the recognition capacity of its mutants, generated by point mutation strategy similar to PheRS, toward methionine(Met) analogues was investigated in vitro.