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Genetic-code evolution for protein synthesis with non-natural amino acids. 2011
Takahito Mukai, and
Tatsuo Yanagisawa, and
Kazumasa Ohtake, and
Masatoshi Wakamori, and
Jiro Adachi, and
Nobumasa Hino, and
Aya Sato, and
Takatsugu Kobayashi, and
Akiko Hayashi, and
Mikako Shirouzu, and
Takashi Umehara, and
Shigeyuki Yokoyama, and
Kensaku Sakamoto
RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan.
The genetic encoding of synthetic or "non-natural" amino acids promises to diversify the functions and structures of proteins. We applied rapid codon-reassignment for creating Escherichia coli strains unable to terminate translation at the UAG "stop" triplet, but efficiently decoding it as various tyrosine and lysine derivatives. This complete change in the UAG meaning enabled protein synthesis with these non-natural molecules at multiple defined sites, in addition to the 20 canonical amino acids. UAG was also redefined in the E. coli BL21 strain, suitable for the large-scale production of recombinant proteins, and its cell extract served the cell-free synthesis of an epigenetic protein, histone H4, fully acetylated at four specific lysine sites.
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