A chemical biology route to site-specific authentic protein modifications

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Many essential biological processes are controlled by posttranslational protein modifications. The inability to synthetically attain the diversity enabled by these modifications limits functional studies of many proteins. We designed a three-step approach for installing authentic posttranslational modifications in recombinant proteins. We first use the established O-phosphoserine (Sep) orthogonal translation system to create a Sep-containing recombinant protein. The Sep residue is then dephosphorylated to dehydroalanine (Dha). Last, conjugate addition of alkyl iodides to Dha, promoted by zinc and copper, enables chemoselective carbon-carbon bond formation. To validate our approach, we produced histone H3, ubiquitin, and green fluorescent protein variants with site-specific modifications, including different methylations of H3K79. The methylated histones stimulate transcription through histone acetylation. This approach offers a powerful tool to engineer diverse designer proteins
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Issue Date
2016-11
Language
English
Article Type
Article
Citation

SCIENCE, v.354, no.6312, pp.623 - 626

ISSN
0036-8075
DOI
10.1126/science.aah4428
URI
http://hdl.handle.net/10203/214602
Appears in Collection
CH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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