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Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses.
| Title | Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses. |
| Publication Type | Journal Article |
| Year of Publication | 2008 |
| Authors | Takahasi, K, Yoneyama, M, Nishihori, T, Hirai, R, Kumeta, H, Narita, R, Gale, M, Inagaki, F, Fujita, T |
| Journal | Mol Cell |
| Volume | 29 |
| Issue | 4 |
| Pagination | 428-40 |
| Date Published | 2008 Feb 29 |
| ISSN | 1097-4164 |
| Keywords | Amino Acid Sequence, Amino Acid Substitution, Animals, DEAD-box RNA Helicases, Gene Expression Regulation, Humans, Immune System, Interferon Regulatory Factor-3, Interferons, Mice, Mice, Knockout, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Nucleic Acid Conformation, Oligonucleotides, Protein Binding, Protein Conformation, Protein Structure, Tertiary, RNA, Double-Stranded, RNA, Viral, Sequence Alignment |
| Abstract | A DExD/H protein, RIG-I, is critical in innate antiviral responses by sensing viral RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded (ds) and 5'ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5'ppp ssRNA in the presence of ATP produces a common structure, as suggested by protease digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD) recognizes these RNA patterns and CTD coincides with the autorepression domain. Structural analysis of CTD by NMR spectroscopy in conjunction with mutagenesis revealed that the basic surface of CTD with a characteristic cleft interacts with RIG-I ligands. Our results suggest that the bipartite structure of CTD regulates RIG-I on encountering viral RNA patterns. |
| DOI | 10.1016/j.molcel.2007.11.028 |
| Alternate Journal | Mol. Cell |
| PubMed ID | 18242112 |
