西亚试剂：Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 In

Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family

Jixin Cui,1,2 Qing Yao,2 Shan Li,2 Xiaojun Ding,2 Qiuhe Lu,2 Haibin Mao,3 Liping Liu,2 Ning Zheng,3,4 She Chen,2 Feng Shao2,*

A family of bacterial effectors including CHBP from Burkholderia pseudomallei and Cif from Enteropathogenic Escherichia coli (EPEC) adopt a functionally important papain-like hydrolytic fold. We show here that CHBP was a potent inhibitor of the eukaryotic ubiquitination pathway. CHBP acted as a deamidase that specifically and efficiently deamidated Gln-40 in ubiquitin and ubiquitin-like protein NEDD8 both in vitro and during Burkholderia infection. Deamidated ubiquitin was impaired in supporting ubiquitin-chain synthesis. Cif selectively deamidated NEDD8, which abolished the activity of neddylated Cullin-RING ubiquitin ligases (CRLs). Ubiquitination and ubiquitin-dependent degradation of multiple CRL substrates were impaired by Cif in EPEC-infected cells. Mutations of substrate-contacting residues in Cif abolished or attenuated EPEC-induced cytopathic s of cell cycle arrest and actin stress fiber formation.

1 Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.

2 National Institute of Biological Sciences, Beijing, 102206, China.

3 Department of Pharmacology, Box 357280, University of Washington, Seattle, WA 98195, USA.

4 Department of Pharmacology and Howard Hughes Medical Institute, Box 357280, University of Washington, Seattle, WA 98195, USA.

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