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- Title
Identification of a second binding site on the TRIM25 B30.2 domain.
- Authors
D'Cruz, Akshay A.; Kershaw, Nadia J.; Hayman, Thomas J.; Linossi, Edmond M.; Chiang, Jessica J.; Wang, May K.; Dagley, Laura F.; Kolesnik, Tatiana B.; Jian-Guo Zhang; Masters, Seth L.; Griffin, Michael D. W.; Gack, Michaela U.; Murphy, James M.; Nicola, Nicos A.; Babon, Jeffrey J.; Nicholson, Sandra E.
- Abstract
The retinoic acid-inducible gene-I (RIG-I) receptor recognizes short 50-di- and triphosphate base-paired viral RNA and is a critical mediator of the innate immune response against viruses such as influenza A, Ebola, HIV and hepatitis C. This response is reported to require an orchestrated interaction with the tripartite motif 25 (TRIM25) B30.2 proteininteraction domain. Here, we present a novel second RIG-I-binding interface on the TRIM25 B30.2 domain that interacts with CARD1 and CARD2 (caspase activation and recruitment domains) of RIG-I and is revealed by the removal of an N-terminal α-helix that mimics dimerization of the full-length protein. Further characterization of the TRIM25 coiled-coil and B30.2 regions indicated that the B30.2 domains move freely on a flexible tether, facilitating RIG-I CARD recruitment. The identification of a dual binding mode for the TRIM25 B30.2 domain is a first for the SPRY/B30.2 domain family and may be a feature of other SPRY/B30.2 family members.
- Subjects
TRIM proteins; BINDING sites; PROTEOMICS; TRETINOIN; RETINOIC acid receptors
- Publication
Biochemical Journal, 2018, Vol 475, Issue 2, p429
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BCJ20170427