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Nucleic Acids Symposium Series 2006 50(1):37-38; doi:10.1093/nass/nrl019
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© 2006 Oxford University Press

Efforts toward codon table engineering: Expansion of unnatural substrates acceptable by the E. coli ribosome

Shinsuke Sando, Kenji Abe, Nobuhiko Sato, Toshihiro Shibata, Keigo Mizusawa and Yasuhiro Aoyama

Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan

The ribosome catalyzes oligo/polymerization of amino acids. We designed an allowable modification of amino acid backbone, based on the hypothesized mechanism of peptidyl transfer reaction. Nonsense suppression method was used to investigate the acceptability of these substrates in the prokaryotic ribosomal system. The E.coli ribosome showed a restricted tolerance to the backbone modification, especially for main-chain elongation. However, our designed homologous ß-hydroxyalkanoic acid with elongated methylene (backbone) chain-length was revealed to be a possible substrate for the E.coli ribosome.


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