Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 15, Issue 3, Pages 387-391Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.cbpa.2011.03.007
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Funding
- National Institute of General Medical Sciences
- National Institutes of Health [GM061796]
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The discovery of pyrrolysine not only expanded the set of the known proteinogenic amino acids but also revealed unusual features of its encoding mechanism. The engagement of a canonical stop codon and a unique aminoacyl-tRNA synthetase-tRNA pair that can be used to accommodate a broad range of unnatural amino acids while maintaining strict orthogonality in a variety of prokaryotic and eukaryotic expression systems has proven an invaluable combination. Within a few years since its properties were elucidated, the pyrrolysine translational machinery has become a popular choice for the synthesis of recombinant proteins bearing a wide variety of otherwise hard-to-introduce functional groups. It is also central to the development of new synthetic strategies that rely on stop-codon suppression.
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