DUB 刀片发出嘶嘶声：军团菌效应蛋白对泛素的新型切割。
The DUB blade goes snicker-snack: Novel ubiquitin cleavage by a Legionella effector protein.
机构信息
Departments of Molecular Biophysics &Biochemistry.
Molecular, Cellular, and Developmental Biology, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.
出版信息
Cell Res. 2017 Jul;27(7):845-846. doi: 10.1038/cr.2017.80. Epub 2017 Jun 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.
摘要
最近，一项研究表明，嗜肺军团菌效应蛋白具有一种前所未有的、不依赖于 ATP 的泛素连接酶活性，可将磷酸核糖基化的泛素（PR-Ub）连接到宿主蛋白的丝氨酸残基上。邱等在《细胞研究》上发表的一项新研究揭示，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来催化 PR-Ub 的去泛素化。
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