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Cell Res. 2017 Jul;27(7):845-846. doi: 10.1038/cr.2017.80. Epub 2017 Jun 2.

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

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1
Departments of Molecular Biophysics &Biochemistry.
2
Molecular, Cellular, and Developmental Biology, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.

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.

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