The DUB blade goes snicker-snack： Novel ubiquitin cleavage by a Legionella effector protein  

作　　者：Judith A Ronau Mark Hochstrasser 

机构地区：[1]Departments of Molecular Biophysics & Biochemistry [2]Molecular, Celhdar, and Developmental Biology, Yale University 266 Whimey Avenue, New Haven, CT06520-8114. USA

出　　处：《Cell Research》2017年第7期845-846,共2页细胞研究（英文版）

摘　　要：Recently, a Legionellapneumophila effector protein was shown to have an unprecedented ATP-independent ubiquitin ligase activity that couples phosphoribosylated ubiquitin （PR- Ub） to serine residues of host pro- teins. A new study published in Cell Research by Qiu et al.reveals that anothar Legionella effector protein, SidJ, catalyzes deubiquitination of PR-Ub by cleavage of the substrate- linked phosphodiester bond.

分 类 号：Q[生物学]