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Structural diversity and oligomerization of bacterial ubiquitin-like proteins
Open accessPreprint — published as 10.1016/j.str.2025.03.011 · Paper page
Abstract
Summary: 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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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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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
- openRxiv
- Published
- 2024-11-21
- Volume
- 33
- Issue
- 6
- Pages
- 1016-1026.e4
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC12145246
- OpenAlex
- W4409540815
- Cited by
- 7
- References
- 1
- Citations by year
- 2026: 3 · 2025: 4
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- 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
- Howard Hughes Medical Institute
- U.S. Department of Energy (DE‐ AC02‐06CH11357, -AC02-05CH11231, AC02‐06CH11357, 05CH11231, P30 GM124165, DE AC02 05CH11231, 06CH11357, GM124169, DE-AC02-)
- National Institutes of Health (DE-AC02–05CH11231, DE-AC02–06CH11357, 1s10od021832-01, GM124165, GM124169)
- Office of Science (AC02‐06CH11357, S10OD021832, DEAC02–05CH11231, AC02-05CH11231, DE-AC02, 06CH11357, DE-AC02-06CH11357)
- University of California, San Diego
- National Institute of General Medical Sciences (DE-AC02-05CH11231, DE-AC02-06CH11357, GM124169, GM144121, GM124165, P30GM124169, R35GM144121, T32GM139795, P30GM124165)
- National Institute of Allergy and Infectious Diseases (F31AI194603)
- Argonne National Laboratory (DE- AC02-06-CH11357, DE-AC02, AC02–06CH11357, DE-AC02-05CH11231, 06CH11357, P30 GM124165)
- Lawrence Berkeley National Laboratory (AC02‐05CH11231, DE-AC02-05CH11231, DE-AC02-06CH11357, 05CH11231)
- 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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