Abstract
Expanding the limited set of 20 amino acids may lead to the generation of proteins with novel properties. Two papers published in the 20 April edition of Science indicate how to accomplish the incorporation of novel amino acids into proteins. The paper by Volker Döring et al., describes the production of mutants of Escherichia coli that incorrectly charge tRNA–valine with cysteine. More than 20% of the valine in cellular proteins in such a mutant organism could be replaced with another amino acid, aminobutyrate, which is similar in shape to cysteine, but is not used in the construction of proteins. The other paper, by Lei Wang et al., describes the construction of a unique tRNA–aminoacyl-tRNA synthetase pair, that, when introduced into E. coli, leads to the in vivo incorporation of the synthetic amino acid O–methyl–l–tyrosine. Using this approach, it is possible to introduce novel amino acids into proteins at any position of interest. DM
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