A functional screen for ubiquitin regulation identifies an E3 ligase secreted by Pseudomonas aeruginosa.

ABSTRACT: Ubiquitin signaling controls many aspects of eukaryotic biology, including targeted protein degradation and immune defense. Remarkably, invading bacterial pathogens have adapted secreted effector proteins that hijack host ubiquitination to gain control over host responses. These ubiquitin-targeted effectors can exhibit, for example, E3 ligase or deubiquitinase activities, often without any sequence or structural homology to eukaryotic ubiquitin regulators. Such convergence in function poses a challenge to the discovery of additional bacterial virulence factors that target ubiquitin. To overcome this, we have developed a workflow to harvest natively secreted bacterial effectors and functionally screen them for ubiquitin regulatory activities. After benchmarking this approach on diverse liga

SUBMITTER: Roberts CG 

PROVIDER: S-EPMC11430079 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature