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Genetic-code evolution for protein synthesis with non-natural amino acids.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

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

doi

10.1016/j.bbrc.2011.07.020

subject

Has Abstract

pub_date

2011-08-12 00:00:00

pages

757-61

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)01239-3

journal_volume

411

pub_type

杂志文章

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