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Volume 27, No 7, Jul 2017

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 27 Issue 7, July 2017: 845-846

RESEARCH HIGHLIGHTS

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

Judith A Ronau1 and Mark Hochstrasser1,2

1Departments of Molecular Biophysics & Biochemistry
2Molecular, Cellular, and Developmental Biology, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA
Correspondence: Mark Hochstrasser,(mark.hochstrasser@yale.edu)

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.


10.1038/cr.2017.80

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