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Ubiquitin-like cGAS chain formation by a super enzyme activates anti-phage response
Open accessPreprint — published as 10.1038/s41564-024-01684-z · Paper page
Abstract
The cyclic oligonucleotide-based anti-phage signaling system (CBASS) is a family of defense system in prokaryotes 1, 2 . Composed of a cyclic GMP-AMP synthase (cGAS) and CBASS-associated proteins, CBASS utilizes cyclic oligonucleotides to activate antiviral immunity 3–6 . One major group of CBASS-associated proteins are homologs of eukaryotic E2 ubiquitin-conjugating enzymes. However, the function of E2 in CBASS remains elusive. Here, we report that a bacterial E2 enzyme regulates cGAS by imitating the entire ubiquitination cascade. This includes the processing of the cGAS C-terminus, conjugation of cGAS to a cysteine residue, ligation of cGAS to a lysine residue, cleavage of the isopeptide bond, and poly-cGASylation. The poly-cGASylation fully activates cGAS to produce cGAMP, which acts as an antiviral signal and leads to cell death. Our findings reveal unique regulatory roles of E2 in CBASS and provide insights into the origin of the ubiquitin system.
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Metadata
- Authors
- Yan, Y., Xiao, J., Huang, F., Yu, B., Cheng, R., Wu, H., Lu, X., Wang, X., Oyejobi, G. K., Robinson, C. V., Wu, H., Wu, D., Wang, L., & Zhu, B.
- Affiliations
- Huazhong University of Science and Technology (CN)
- Wuhan University (CN)
- Boston Children's Hospital (US)
- University of Oxford (GB)
- Corresponding author
- Huang, Fengtao
- Wu, Di
- Wang, Longfei
- Zhu, Bin
- ORCID
- Venue
- Nature Microbiology
- Publisher
- openRxiv
- Published
- 2022-05-25
- Volume
- 9
- Issue
- 6
- Pages
- 1566-1578
- ISSN
- 2058-5276 (ISSN-L)
- OpenAlex
- W4395010496
- Cited by
- 29
- References
- 1
- Citations by year
- 2026: 6 · 2025: 14 · 2024: 6 · 2023: 3
- FWCI
- 7.13
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature Microbiology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Research Square (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31900032, 31870165, 22174003, 21974002, 32150009)
- Science, Technology and Innovation Commission of Shenzhen Municipality (JCYJ20210324115811032)
- National Key Research and Development Program of China
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- C-BASS, cGAS, E2 ubiquitin-conjugating enzyme, Serratia marcescens, cGAMP, antiviral innate immunity, phage defense, cell death
- MeSH terms
- Cyclic Guanosine Monophosphate-Adenosine Monophosphate Synthase, Bacterial Proteins, Bacteriophages, Humans, Immunity, Innate, Nucleotides, Cyclic, Nucleotidyltransferases, Signal Transduction, Cryoelectron Microscopy, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitination
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