Efficient introduction of alkene functionality into proteins in vivo

J.C.M. Hest, van, D.A. Tirrell

Research output: Contribution to journalArticleAcademicpeer-review

75 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)68-70
Number of pages3
JournalFEBS Letters
Volume428
Issue number1-2
DOIs
Publication statusPublished - 22 May 1998
Externally publishedYes

Keywords

  • Amino acid analogue
  • Chemical modification
  • Homoallylglycine
  • Methionine replacement
  • Protein engineering

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