Traceless and site-specific ubiquitination of recombinant proteins

Satpal Virdee, Prashant B. Kapadnis, Thomas Elliott, Kathrin Lang, Julia Madrzak, Duy P. Nguyen, Lutz Riechmann, Jason W. Chin

Research output: Contribution to journalArticlepeer-review

154 Scopus citations


Protein ubiquitination is a post-translational modification that regulates almost all aspects of eukaryotic biology. Here we discover the first routes for the efficient site-specific incorporation of δ-thiol-l-lysine (7) and δ-hydroxy-l-lysine (8) into recombinant proteins, via evolution of a pyrrolysyl-tRNA synthetase/tRNACUA pair. We combine the genetically directed incorporation of 7 with native chemical ligation and desulfurization to yield an entirely native isopeptide bond between substrate proteins and ubiquitin. We exemplify this approach by demonstrating the synthesis of a ubiquitin dimer and the first synthesis of ubiquitinated SUMO.

Original languageEnglish
Pages (from-to)10708-10711
Number of pages4
JournalJournal of the American Chemical Society
Issue number28
StatePublished - 20 Jul 2011
Externally publishedYes


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