title: Efforts toward codon table engineering: expansion of unnatural substrates acceptable by the E. coli ribosome.
abstract: 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 beta-hydroxyalkanoic acid with elongated methylene (backbone) chain-length was revealed to be a possible substrate for the E.coli ribosome.
authors.affiliation: Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
authors.forename: Shinsuke
authors.initials: S
authors.lastname: Sando
authors.forename: Kenji
authors.initials: K
authors.lastname: Abe
authors.forename: Nobuhiko
authors.initials: N
authors.lastname: Sato
authors.forename: Toshihiro
authors.initials: T
authors.lastname: Shibata
authors.forename: Keigo
authors.initials: K
authors.lastname: Mizusawa
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Aoyama
mesh_terms: D003062:Codon; D004926:Escherichia coli / Q000235:genetics*; D011422:Propionates / Q000378:metabolism; D014176:Protein Biosynthesis; D015202:Protein Engineering / Q000379:methods*; D012270:Ribosomes / Q000378:metabolism*
chemical_list: D003062:Codon; D011422:Propionates