Reference - Detail
| 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 |
| WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Patent(IFI CLAIMS) |
| Total number of mentions | 8 |
| Altmetric score changes over past 6months | 3.0 |
| Resource | |
| Prokaryotes E. coli | ME9062(BW25113) |