A eukaryotic-like ubiquitination system in bacterial antiviral defence.

ABSTRACT: Ubiquitination pathways have crucial roles in protein homeostasis, signalling 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 operon associated with phage defence islands encodes a complete ubiquitination pathway. Two structures of a bacterial E1-E2-Ubl complex reveal striking architectural parallels with canonical eukaryotic ubiquitination machin

SUBMITTER: Chambers LR 

PROVIDER: S-EPMC11476048 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature