| Literature DB >> 28574056 |
Judith A Ronau1, Mark Hochstrasser1,2.
Abstract
Recently, a Legionella pneumophila effector protein was shown to have an unprecedented ATP-independent ubiquitin ligase activity that couples phosphoribosylated ubiquitin (PR-Ub) to serine residues of host proteins. A new study published in Cell Research by Qiu et al. reveals that another Legionella effector protein, SidJ, catalyzes deubiquitination of PR-Ub by cleavage of the substrate-linked phosphodiester bond.Entities:
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Year: 2017 PMID: 28574056 PMCID: PMC5518992 DOI: 10.1038/cr.2017.80
Source DB: PubMed Journal: Cell Res ISSN: 1001-0602 Impact factor: 25.617