Nonprotein amino acid furanomycin, unlike isoleucine in chemical structure, is charged to isoleucine tRNA by isoleucyl-tRNA synthetase and incorporated into protein

T. Kohno, Daisuke Kohda, M. Haruki, S. Yokoyama, T. Miyazawa

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Abstract

Nonprotein amino acid furanomycin was found to bind with Escherichia coli isoleucyl-tRNA synthetase (IleRS) almost as tightly as the substrate L-isoleucine. The conformation of furanomycin bound to the enzyme was determined by NMR analyses including the transferred nuclear Overhauser effect method. The conformation of IleRS-bound furanomycin was similar to that of L-isoleucine, although the chemical structure of furanomycin is unlike that of L-isoleucine. By E. coli IleRS, E. coli tRNA(Ile) was charged with furanomycin as efficiently as with L-isoleucine. Furthermore, furanomycyl-tRNA(Ile) was bound to polypeptide chain elongation factor Tu as tightly as isoleucyl-tRNA(Ile). Furanomycin was found to be incorporated into β-lactamase precursor by in vitro protein biosynthesis. A newly designed amino acid will probably be incorporated into proteins, provided that the new amino acid takes a similar conformation as a protein-constituting amino acid in the active site of an aminoacyl-tRNA synthetase.

Original languageEnglish
Pages (from-to)6931-6935
Number of pages5
JournalJournal of Biological Chemistry
Volume265
Issue number12
Publication statusPublished - May 16 1990
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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