Bacterial antiviral defense pathways encode eukaryotic-like ubiquitination systems.

ABSTRACT: Ubiquitination and related pathways play crucial roles in protein homeostasis, signaling, and innate immunity^1-3. In these pathways, an enzymatic cascade of E1, E2, and E3 proteins conjugates ubiquitin or a ubiquitin-like protein (Ubl) to target-protein lysine residues⁴. Bacteria encode ancient relatives of E1 and Ubl proteins involved in sulfur metabolism^5,6 but these proteins do not mediate Ubl-target conjugation, leaving open the question of whether bacteria can perform ubiquitination-like protein conjugation. Here, we demonstrate that a bacterial antiviral immune system encodes a complete ubiquitination pathway. Two structures of a bacterial E1:E2:Ubl complex reveal striking architectural parallels with canonical eukaryotic ubiquitination machinery. The

SUBMITTER: Chambers LR 

PROVIDER: S-EPMC10557695 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature