Journal
FEBS LETTERS
Volume 502, Issue 1-2, Pages 25-30Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02657-6
Keywords
methionyl-tRNA synthetase; protein; engineering; methionine; non-natural amino acid
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Amino acid incorporation into proteins in vivo is controlled most stringently by the aminoacyl-tRNA synthetases. Here we report the incorporation of several new methionine analogues into protein by increasing the rate of their activation by the methionyl-tRNA synthetase (MetRS) of Escherichia coli. cis-Crotylglycine (4), 2-aminoheptanoic acid (7), norvaline (8), 2-butynylglycine (11), and allylglycine (12) will each support protein synthesis in methionine-depleted cultures of E. coli when MetRS is overexpressed and the medium is supplemented with the analogue at millimolar concentrations. These investigations suggest important opportunities for protein engineering, as expansion of the translational apparatus toward other amino acid analogues by similar strategies should also be possible. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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