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- Title
Recombinant expression of selectively sulfated proteins in Escherichia coli.
- Authors
Liu, Chang C.; Schultz, Peter G.
- Abstract
Although tyrosine sulfation is a post-translational modification widespread across multicellular eukaryotes, its biological functions remain largely unknown. This is in part due to the difficulties of synthesizing selectively sulfated proteins. Here we report the selective incorporation of sulfotyrosine into proteins in bacteria by genetically encoding the modified amino acid in response to the amber nonsense codon TAG. Moreover, we show that this strategy enables direct expression in Escherichia coli of sulfo-hirudin, previously inaccessible through recombinant methods. The affinity of sulfo-hirudin toward human thrombin is enhanced more than tenfold over that of desulfo-hirudin, suggesting that sulfo-hirudin may offer clinical advantages for use as an anticoagulant. This general approach to the biosynthesis of sulfated proteins should facilitate further study and application of tyrosine sulfation.
- Subjects
ESCHERICHIA coli; ANTICOAGULANTS; RECOMBINANT proteins; THROMBIN; BIOSYNTHESIS
- Publication
Nature Biotechnology, 2006, Vol 24, Issue 11, p1436
- ISSN
1087-0156
- Publication type
Article
- DOI
10.1038/nbt1254