RRC ID |
47434
|
著者 |
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.
|
タイトル |
Genetic-code evolution for protein synthesis with non-natural amino acids.
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ジャーナル |
Biochem Biophys Res Commun
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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.
|
巻・号 |
411(4)
|
ページ |
757-61
|
公開日 |
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
|
引用数 |
52
|
WOS 分野
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
リソース情報 |
遺伝子材料 |
BW25113-based RFzero-iy (RDB14427)
BL21(DE3)-based RFzero-iy (RDB14428). |
原核生物(大腸菌) |
|