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Caenorhabditis elegans Dicer acts with the RIG-I-like helicase DRH-1 and RDE-4 to cleave dsRNA
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Abstract
Invertebrates use the endoribonuclease Dicer to cleave viral dsRNA during antiviral defense, while vertebrates use RIG-I-like Receptors (RLRs), which bind viral dsRNA to trigger an interferon response. While some invertebrate Dicers act alone during antiviral defense, Caenorhabditis elegans Dicer acts in a complex with a dsRNA binding protein called RDE-4, and an RLR ortholog called DRH-1. We used biochemical and structural techniques to provide mechanistic insight into how these proteins function together. We found RDE-4 is important for ATP-independent and ATP-dependent cleavage reactions, while helicase domains of both DCR-1 and DRH-1 contribute to ATP-dependent cleavage. DRH-1 plays the dominant role in ATP hydrolysis, and like mammalian RLRs, has an N-terminal domain that functions in autoinhibition. A cryo-EM structure indicates DRH-1 interacts with DCR-1’s helicase domain, suggesting this interaction relieves autoinhibition. Our study unravels the mechanistic basis of the collaboration between two helicases from typically distinct innate immune defense pathways.
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Metadata
- Authors
- Consalvo, C. D., Aderounmu, A. M., Donelick, H. M., Aruscavage, P. J., Eckert, D. M., Shen, P. S., & Bass, B. L.
- Affiliations
- University of Utah (US)
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2024-05-15
- Volume
- 13
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W4396924679
- Cited by
- 12
- References
- 79
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 4
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- creativecommons.org/licenses/by/4.0/ (vor)
- creativecommons.org/licenses/by/4.0/ (am)
- creativecommons.org/licenses/by/4.0/ (tdm)
- Locations
- eLife (publishedVersion, cc-by)
- Funders
- National Institute of General Medical Sciences (R35GM141262, R35GM133772)
- National Cancer Institute (R01CA260414)
- National Institutes of Health (T32AI055434)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Keywords
- Caenorhabditis elegans, Dicer, RIG-I-like helicases, double-stranded RNA cleavage, antiviral innate immunity, ATP hydrolysis, autoinhibition, helicase domain, cryo-EM structure, protein complex structure
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