Incorporations of unnatural amino acids in proteins are a useful technique in medical and industrial fields. For practical usages, misacylation caused by engineered aminoacyl-tRNA synthetases can be one of the issues lowering the purity of the generated proteins. Since acceptor stems of tRNAs are known to possess identity elements specific for each amino acid, the misacylation is probably caused by non-specificity of the acceptor stems in tRNAs. In this paper, we modified an acceptor stem of tRNA
Tyr, and tested aminoacylation of over 100 modified tRNAs. Finally, we found the acceptor stem sequence for the tRNA with less misacylation for both tyrosine and tyrosine derivative unnatural amino acids.
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