Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3).
Amino Acid Sequence
Animals
Caenorhabditis elegans
/ genetics
Caenorhabditis elegans Proteins
/ metabolism
Crystallography, X-Ray
DEAD Box Protein 58
/ metabolism
DEAD-box RNA Helicases
/ metabolism
Interferon-Induced Helicase, IFIH1
/ metabolism
Protein Domains
/ genetics
RNA Interference
RNA, Double-Stranded
/ genetics
RNA-Binding Proteins
/ metabolism
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
27 09 2021
27 09 2021
Historique:
accepted:
03
08
2021
revised:
31
07
2021
received:
04
03
2021
pubmed:
18
8
2021
medline:
21
12
2021
entrez:
17
8
2021
Statut:
ppublish
Résumé
DRH-3 is critically involved in germline development and RNA interference (RNAi) facilitated chromosome segregation via the 22G-siRNA pathway in Caenorhabditis elegans. DRH-3 has similar domain architecture to RIG-I-like receptors (RLRs) and belongs to the RIG-I-like RNA helicase family. The molecular understanding of DRH-3 and its function in endogenous RNAi pathways remains elusive. In this study, we solved the crystal structures of the DRH-3 N-terminal domain (NTD) and the C-terminal domains (CTDs) in complex with 5'-triphosphorylated RNAs. The NTD of DRH-3 adopts a distinct fold of tandem caspase activation and recruitment domains (CARDs) structurally similar to the CARDs of RIG-I and MDA5, suggesting a signaling function in the endogenous RNAi biogenesis. The CTD preferentially recognizes 5'-triphosphorylated double-stranded RNAs bearing the typical features of secondary siRNA transcripts. The full-length DRH-3 displays unique structural dynamics upon binding to RNA duplexes that differ from RIG-I or MDA5. These features of DRH-3 showcase the evolutionary divergence of the Dicer and RLR family of helicases.
Identifiants
pubmed: 34403472
pii: 6353803
doi: 10.1093/nar/gkab712
pmc: PMC8464030
doi:
Substances chimiques
Caenorhabditis elegans Proteins
0
RNA, Double-Stranded
0
RNA-Binding Proteins
0
Drh-3 protein, C elegans
EC 2.7.7.-
DEAD Box Protein 58
EC 3.6.4.13
DEAD-box RNA Helicases
EC 3.6.4.13
Interferon-Induced Helicase, IFIH1
EC 3.6.4.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
9978-9991Subventions
Organisme : Howard Hughes Medical Institute
Pays : United States
Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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