Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary

Mark A Nakasone, Danny T Huang (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.

Original languageEnglish
Pages (from-to)807-809
Number of pages3
JournalMolecular Cell
Issue number6
Early online date16 Jun 2016
Publication statusPublished - 16 Jun 2016


  • ADP Ribose Transferases
  • Humans
  • Legionella pneumophila/enzymology
  • Ubiquitin
  • Ubiquitin-Conjugating Enzymes/genetics
  • Ubiquitination


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