Sensing viral RNAs by Dicer/RIG-I like ATPases across species.
Fiche publication
Date publication
février 2015
Journal
Current opinion in immunology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr IMLER Jean-Luc, Dr MEIGNIN Carine
Tous les auteurs :
Paro S, Imler JL, Meignin C
Lien Pubmed
Résumé
Induction of antiviral immunity in vertebrates and invertebrates relies on members of the RIG-I-like receptor and Dicer families, respectively. Although these proteins have different size and domain composition, members of both families share a conserved DECH-box helicase domain. This helicase, also known as a duplex RNA activated ATPase, or DRA domain, plays an important role in viral RNA sensing. Crystallographic and electron microscopy studies of the RIG-I and Dicer DRA domains indicate a common structure and that similar conformational changes are induced by dsRNA binding. Genetic and biochemical studies on the function and regulation of DRAs reveal similarities, but also some differences, between viral RNA sensing mechanisms in nematodes, flies and mammals.
Mots clés
Adenosine Triphosphatases, metabolism, Animals, DEAD-box RNA Helicases, chemistry, Humans, Protein Binding, Protein Interaction Domains and Motifs, RNA, Viral, chemistry, Ribonuclease III, chemistry, Virus Diseases, immunology, Viruses, immunology
Référence
Curr. Opin. Immunol.. 2015 Feb;32:106-13