Identification of an expanded set of translationally active methionine analogues in Escherichia coli

FEBS Letters

Tirrell, D.A.¹  Kiick, K.L.²  Weberskirch, R.¹ 

[1] Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA;Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA

关键词: Methionyl-tRNA synthetase;    Protein engineering;    Methionine;    Non-natural amino acid;   

DOI  :  10.1016/S0014-5793(01)02657-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown