Published May 22, 1998
| Published
Journal Article
Open
Efficient introduction of alkene functionality into proteins in vivo
- Creators
- van Hest, Jan C. M.
- Tirrell, David A.
Abstract
The methionine analogue 2-amino-5-hexenoic acid (homoallylglycine, Hag) can be utilized by Escherichia coli in the initiation and elongation steps of protein biosynthesis. Use of an E. coli methionine auxotroph and Hag-supplemented medium resulted in replacement of ca. 85% of the methionine residues in mouse dihydrofolate reductase expressed under control of a bacteriophage T5 promoter. N-terminal sequencing indicated 92±5% occupancy of the initiator site by Hag. The vinyl function of Hag remains intact in the purified protein and suggests new chemistries for modification of natural and artificial proteins prepared in bacterial hosts.
Additional Information
© 1998 Federation of European Biochemical Societies. Received 9 March 1998; revised version received 9 April 1998. The authors thank L.C. Dickinson for assistance with NMR spectroscopy and D.C. Rees for bringing to our attention References [23]and [24]. This work was supported by a grant from the Polymers and Genetics Programs of the US National Science Foundation. The Netherlands Organization for Scientific Research (NWO) and DSM-Research are acknowledged for unrestricted research grants.Attached Files
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Additional details
- Eprint ID
- 53435
- Resolver ID
- CaltechAUTHORS:HESfebsl1998
- NSF
- Netherlands Organization for Scientific Research (NWO)
- DSM-Research
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2015-02-06Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field