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Gan, Ninghai; Zhen, Xiangkai; Liu, Yao; Xu, Xiaolong; He, Chunlin; Qiu, Jiazhang; Liu, Yancheng; Fujimoto, Grant M; Nakayasu, Ernesto S; Zhou, Biao; Zhao, Lan; Puvar, Kedar; Das, Chittaranjan; Ouyang, Songying; Luo, Zhao-Qing
Nature (London), 08/2019, Letnik: 572, Številka: 7769Journal Article
The bacterial pathogen Legionella pneumophila creates an intracellular niche permissive for its replication by extensively modulating host-cell functions using hundreds of effector proteins delivered by its Dot/Icm secretion system . Among these, members of the SidE family (SidEs) regulate several cellular processes through a unique phosphoribosyl ubiquitination mechanism that bypasses the canonical ubiquitination machinery . The activity of SidEs is regulated by another Dot/Icm effector known as SidJ ; however, the mechanism of this regulation is not completely understood . Here we demonstrate that SidJ inhibits the activity of SidEs by inducing the covalent attachment of glutamate moieties to SdeA-a member of the SidE family-at E860, one of the catalytic residues that is required for the mono-ADP-ribosyltransferase activity involved in ubiquitin activation . This inhibition by SidJ is spatially restricted in host cells because its activity requires the eukaryote-specific protein calmodulin (CaM). We solved a structure of SidJ-CaM in complex with AMP and found that the ATP used in this reaction is cleaved at the α-phosphate position by SidJ, which-in the absence of glutamate or modifiable SdeA-undergoes self-AMPylation. Our results reveal a mechanism of regulation in bacterial pathogenicity in which a glutamylation reaction that inhibits the activity of virulence factors is activated by host-factor-dependent acyl-adenylation.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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