Comparison of Phosphoribosyl Ubiquitin Probes Targeting <i>Legionella</i> Dup Enzymes.

ABSTRACT: In order to effectively replicate within a host cell, the Legionella pneumophila bacterium secretes effector enzymes into the cytoplasm in order to manipulate cellular host pathways including host ubiquitination. Some of these effectors, the so-called SidE-family, mediate noncanonical phosphoribosyl serine ubiquitination (PR-ubiquitination) of host substrate proteins, contributing to the recruitment of ER-remodeling proteins and the formation of a Legionella-containing vacuole, which is crucial in the early stages of bacterial infection. PR-ubiquitination is a dynamic process that is reversed by other Legionella effectors called deubiquitinases for PR-ubiquitination (Dups). We recently discovered a reactive allosteric cysteine in close proximity to the catalytic triad

SUBMITTER: Kloet MS 

PROVIDER: S-EPMC11926780 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature