Strange New World: Bacteria Catalyze Ubiquitylation via ADP Ribosylation.
Three recent papers, including one by Kotewicz et al. (2016) in this issue of Cell Host & Microbe, show that Legionella deploys a novel form of ubiquitylation to generate its replicative vacuole. Without E1 and E2 enzymes, SidE effectors ubiquitylate serine residues in substrates via an ADP-ribosylated ubiquitin intermediate.
MRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: dk@mrc-lmb.cam.ac.uk.
David
D
Komander
MRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK; University of Cambridge, Department of Medicine, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK. Electronic address: randow@mrc-lmb.cam.ac.uk.
Felix
F
Randow
D000246:Adenosine Diphosphate Ribose; D001419:Bacteria; D006801:Humans; D012694:Serine; D025801:Ubiquitin; D054875:Ubiquitination
D025801:Ubiquitin; D000246:Adenosine Diphosphate Ribose; D012694:Serine