Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-04

AUTHORS

J D Bain, C Switzer, A R Chamberlin, S A Benner

ABSTRACT

One serious limitation facing protein engineers is the availability of only 20 'proteinogenic' amino acids encoded by natural messenger RNA. The lack of structural diversity among these amino acids restricts the mechanistic and structural issues that can be addressed by site-directed mutagenesis. Here we describe a new technology for incorporating non-standard amino acids into polypeptides by ribosome-based translation. In this technology, the genetic code is expanded through the creation of a 65th codon-anticodon pair from unnatural nucleoside bases having non-standard hydrogen-bonding patterns. This new codon-anticodon pair efficiently supports translation in vitro to yield peptides containing a non-standard amino acid. The versatility of the ribosome as a synthetic tool offers new possibilities for protein engineering, and compares favourably with another recently described approach in which the genetic code is simply rearranged to recruit stop codons to play a coding role. More... »

PAGES

537-539

Journal

TITLE

Nature

ISSUE

6369

VOLUME

356

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/356537a0

    DOI

    http://dx.doi.org/10.1038/356537a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1042018906

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1560827


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