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.

中文翻译：

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DUB刀片变得窃窃私语：军团菌效应蛋白可对新型泛素进行切割。

最近，一种嗜肺军团菌效应蛋白被证明具有前所未有的不依赖ATP的泛素连接酶活性，该活性将磷酸核糖化的泛素（PR-Ub）与宿主蛋白的丝氨酸残基偶联。Qiu等在《细胞研究》上发表的一项新研究。揭示了另一种军团菌效应蛋白SidJ通过切割底物连接的磷酸二酯键催化PR-Ub的去泛素化。