Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary.
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.
Cancer Research UK Beatson Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.
Mark A
MA
Nakasone
Cancer Research UK Beatson Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK. Electronic address: d.huang@beatson.gla.ac.uk.
Danny T
DT
Huang
D036002:ADP Ribose Transferases; D006801:Humans; D016952:Legionella pneumophila / Q000201:enzymology; D025801:Ubiquitin; D044763:Ubiquitin-Conjugating Enzymes / Q000235:genetics; D054875:Ubiquitination
D025801:Ubiquitin; D044763:Ubiquitin-Conjugating Enzymes; D036002:ADP Ribose Transferases