Structural diversity and oligomerization of bacterial ubiquitin-like proteins.

ABSTRACT: Bacteria possess a variety of operons with homology to eukaryotic ubiquitination pathways that encode predicted E1, E2, E3, deubiquitinase, and ubiquitin-like proteins. Some of these pathways have recently been shown to function in anti-bacteriophage immunity, but the biological functions of others remain unknown. Here, we show that ubiquitin-like proteins in two bacterial operon families show surprising architectural diversity, possessing one to three β-grasp domains preceded by diverse N-terminal domains. We find that a large group of bacterial ubiquitin-like proteins possess three β-grasp domains and form homodimers and helical filaments mediated by conserved Ca²⁺ ion binding sites. Our findings highlight a distinctive mode of self-assembly for ubiquitin-like proteins, and su

SUBMITTER: Gong M 

PROVIDER: S-EPMC11601603 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature