RRC ID 35408
Author Mukai T, Yanagisawa T, Ohtake K, Wakamori M, Adachi J, Hino N, Sato A, Kobayashi T, Hayashi A, Shirouzu M, Umehara T, Yokoyama S, Sakamoto K.
Title Genetic-code evolution for protein synthesis with non-natural amino acids.
Journal Biochem Biophys Res Commun
Abstract 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.
Volume 411(4)
Pages 757-61
Published 2011-8-12
DOI 10.1016/j.bbrc.2011.07.020
PII S0006-291X(11)01239-3
PMID 21782790
MeSH Amino Acids / chemistry Amino Acids / genetics* Codon, Terminator / genetics Directed Molecular Evolution / methods* Escherichia coli / genetics Escherichia coli Proteins / genetics Evolution, Molecular Gene Knockout Techniques Genetic Code* Histones / genetics Histones / metabolism Peptide Chain Termination, Translational / genetics Peptide Termination Factors / genetics Plasmids / genetics Protein Biosynthesis / genetics*
IF 2.985
Prokaryotes E. coli ME9062(BW25113)