Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase.

ABSTRACT: 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 system¹. Among these, members of the SidE family (SidEs) regulate several cellular processes through a unique phosphoribosyl ubiquitination mechanism that bypasses the canonical ubiquitination machinery^2-4. The activity of SidEs is regulated by another Dot/Icm effector known as SidJ⁵; however, the mechanism of this regulation is not completely understood^6,7. 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

SUBMITTER: Gan N 

PROVIDER: S-EPMC6855250 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature