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Cited by 7Ubiquitin and proteasome pathwaysBacterial Genetics and BiotechnologyEnzyme Structure and Function

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Structural diversity and oligomerization of bacterial ubiquitin-like proteins

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Gong, Minheng, Ye, Qiaozhen, Gu, Yajie, Chambers, Lydia R., Bobkov, Andrey A., Arakawa, Neal K., Matyszewski, Mariusz, Corbett, Kevin D.·2025·Structure
DOI 10.1016/j.str.2025.03.011PMC PMC12145246

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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 Ca 2+ ion binding sites. Our findings highlight a distinctive mode of self-assembly for ubiquitin-like proteins and suggest that Ca 2+-mediated ubiquitin-like protein filament assembly and/or disassembly enables cells to sense and respond to stress conditions that alter intracellular metal ion concentration.

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Metadata

Authors
Gong, M., Ye, Q., Gu, Y., Chambers, L. R., Bobkov, A. A., Arakawa, N. K., Matyszewski, M., & Corbett, K. D.
Affiliations
  • University of California San Diego (US)
  • Sanford Burnham Prebys Medical Discovery Institute (US)
Corresponding author
Corbett, Kevin D.
ORCID
Venue
Structure
Publisher
Elsevier BV
Published
2025-06
Volume
33
Issue
6
Pages
1016-1026.e4
ISSN
0969-2126 (ISSN-L)
DOI
10.1016/j.str.2025.03.011
PMC
PMC12145246
OpenAlex
W4409540815
Cited by
7
References
6
Citations by year
2026: 3 · 2025: 4
FWCI
0.95
Type
journal article
Language
en
Open access
Licence
Locations
  • Structure (acceptedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • Argonne National Laboratory (DE-AC02-06CH11357)
  • Office of Science (DE-AC02-05CH11231, S10OD021832)
  • Howard Hughes Medical Institute
  • U.S. Department of Energy
  • NIH National Institute of General Medical Sciences (P30 GM124165, P30 GM124169, T32 GM139795, R35 GM144121)
  • University of California, San Diego
  • National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
oligomerization, filament assembly, filament disassembly, metal ion sensing, stress response, structural diversity

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