Characterization of DCL4 missense alleles provides insights into its ability to process distinct classes of dsRNA substrates.
Fiche publication
Date publication
avril 2018
Journal
The Plant journal : for cell and molecular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Mr HAMMANN Philippe, Mme COGNAT Valérie
Tous les auteurs :
Montavon T, Kwon Y, Zimmermann A, Hammann P, Vincent T, Cognat V, Bergdoll M, Michel F, Dunoyer P
Lien Pubmed
Résumé
In the model plant Arabidopsis thaliana, four Dicer-like proteins (DCL1-4) mediate the production of various classes of small RNAs (sRNAs). Among these four proteins, DCL4 is by far the most versatile RNaseIII-like enzyme and previously identified dcl4 missense alleles were shown to uncouple the production of the various classes of DCL4-dependent sRNAs. Yet, little is known about the molecular mechanism pertaining this uncoupled production. Here, by studying the subcellular localization, interactome and binding to the sRNA precursors of three distinct dcl4 missense alleles, we simultaneously highlight the absolute requirement of a specific residue in its helicase domain for efficient production of all DCL4-dependent sRNAs, and identify, within its PAZ domain, an important determinant of DCL4 versatility that is mandatory for efficient processing of intramolecular foldback dsRNA precursors but dispensable for the production of siRNAs from RDR-dependent dsRNA susbtrates. This study not only provides insights into DCL4 mode of action but also delineates interesting tools to further study the complexity of RNA silencing pathways in plants and possibly other organisms. This article is protected by copyright. All rights reserved.
Mots clés
Arabidopsis thaliana , DCL4, Helicase domain, PAZ domain, RNA silencing, siRNA
Référence
Plant J.. 2018 Apr 22;: