Identification of an expanded set of translationally active methionine analogues in Escherichia coli
- Creators
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Kiick, K. L.
- Weberskirch, R.
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Tirrell, D. A.
Abstract
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.
Additional Information
© 2001 Elsevier. Received 6 June 2001; accepted 13 June 2001. First published online 9 July 2001. This work was supported by grants from the Polymers and Genetics Programs of the U.S. National Science Foundation and from the U.S. Army Research Office. We are grateful to J.C.M. van Hest and to H. Blackwell for synthesis of methionine analogues and to H. Jakubowski and Y. Mechulam for donation of plasmids encoding MetRS. K.L.K. thanks the U.S. Department of Defense for a National Defense Science and Engineering Graduate Fellowship.Errata
Corrigendum to: Identification of an expanded set of translationally active methionine analogues in Escherichia coli (FEBS 25068): [FEBS Letters 502 (2001) 25–30] K.L. Kiick, R. Weberskirch, D.A. TirrellAttached Files
Published - 199-Kiick.pdf
Erratum - 1-s2.0-S0014579301028575-main.pdf
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Additional details
- Eprint ID
- 53353
- Resolver ID
- CaltechAUTHORS:KIIfl2001
- NSF
- Army Research Office (ARO)
- National Defense Science and Engineering Graduate (NDSEG) Fellowship
- Created
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2015-02-07Created from EPrint's datestamp field
- Updated
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2023-06-01Created from EPrint's last_modified field