Molecular basis of Gabija anti-phage supramolecular assemblies
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Abstract
As one of the most prevalent anti-phage defense systems in prokaryotes, Gabija consists of a Gabija protein A (GajA) and a Gabija protein B (GajB). The assembly and function of the Gabija system remain unclear. Here we present cryo-EM structures of Bacillus cereus GajA and GajAB complex, revealing tetrameric and octameric assemblies, respectively. In the center of the complex, GajA assembles into a tetramer, which recruits two sets of GajB dimer at opposite sides of the complex, resulting in a 4:4 GajAB supramolecular complex for anti-phage defense. Further biochemical analysis showed that GajA alone is sufficient to cut double-stranded DNA and plasmid DNA, which can be inhibited by ATP. Unexpectedly, the GajAB displays enhanced activity for plasmid DNA, suggesting a role of substrate selection by GajB. Together, our study defines a framework for understanding anti-phage immune defense by the GajAB complex.
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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 · see citing works
Diversity, classification and evolution of CRISPR-Cas systems
Koonin, E. V., Makarova, K. S., & Zhang, F. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.05.008 · Cited by 1,423 · see citing works
Structural basis of Gabija anti-phage defence and viral immune evasion
Antine, S. P., Johnson, A. G., Mooney, S. E., Leavitt, A., Mayer, M. L., Yirmiya, E., Amitai, G., Sorek, R., & Kranzusch, P. J. (2024) · Nature · doi:10.1038/s41586-023-06855-2 · Cited by 125 · see citing works
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- Authors
- Yang, X.-Y., Shen, Z., Xie, J., Greenwald, J., Marathe, I., Lin, Q., Xie, W. J., Wysocki, V. H., & Fu, T.-M.
- Affiliations
- The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute (US)
- The Ohio State University (US)
- University of Florida (US)
- Corresponding author
- Fu, Tian-Min
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2024-04-16
- Volume
- 31
- Issue
- 8
- Pages
- 1243-1250
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC11418746
- OpenAlex
- W4394855524
- Cited by
- 23
- References
- 3
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 5
- FWCI
- 6.31
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- Research Square (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (GM 103310)
- National Cancer Institute
- National Institute of General Medical Sciences (P41GM103310, GM103310, R35GM147465)
- Topics
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- anti-phage defense, supramolecular self-assembly, Bacillus cereus, DNA double-strand breaks, plasmid DNA, ATP inhibition, protein complex stoichiometry, cryo-EM structure
- MeSH terms
- Adenosine Triphosphate, Bacillus cereus, Bacterial Proteins, Models, Molecular, Plasmids, Cryoelectron Microscopy, Protein Multimerization
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