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Traceless and site-specific ubiquitination of recombinant proteins

Traceless and site-specific ubiquitination of recombinant proteins

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Authors

  • Satpal Virdee
  • Prashant B. Kapadnis
  • Thomas Elliott
  • Kathrin Lang
  • Julia Madrzak
  • Duy P. Nguyen
  • Lutz Riechmann
  • Jason W. Chin (Lead / Corresponding author)

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Info

Original languageEnglish
Pages10708-10711
Number of pages4
JournalJournal of the American Chemical Society
Journal publication date20 Jul 2011
Journal number28
Volume133
DOIs
StatePublished

Abstract

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 delta-thiol-L-lysine (7) and delta-hydroxy-L-lysine (8) into recombinant proteins, via evolution of a pyrrolysyl-tRNA synthetase/tRNA(CUA) 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.

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