Abstract
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 language | English |
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Pages (from-to) | 807-809 |
Number of pages | 3 |
Journal | Molecular Cell |
Volume | 62 |
Issue number | 6 |
Early online date | 16 Jun 2016 |
DOIs | |
Publication status | Published - 16 Jun 2016 |
Keywords
- ADP Ribose Transferases
- Humans
- Legionella pneumophila/enzymology
- Ubiquitin
- Ubiquitin-Conjugating Enzymes/genetics
- Ubiquitination