Fiche publication
Date publication
novembre 2024
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Mr HAMMANN Philippe
Tous les auteurs :
Felgines L, Rymen B, Martins LM, Xu G, Matteoli C, Himber C, Zhou M, Eis J, Coruh C, Böhrer M, Kuhn L, Chicher J, Pandey V, Hammann P, Wohlschlegel J, Waltz F, Law JA, Blevins T
Lien Pubmed
Résumé
Eukaryotes must balance the need for gene transcription by RNA polymerase II (Pol II) against the danger of mutations caused by transposable element (TE) proliferation. In plants, these gene expression and TE silencing activities are divided between different RNA polymerases. Specifically, RNA polymerase IV (Pol IV), which evolved from Pol II, transcribes TEs to generate small interfering RNAs (siRNAs) that guide DNA methylation and block TE transcription by Pol II. While the Pol IV complex is recruited to TEs via SNF2-like CLASSY (CLSY) proteins, how Pol IV partners with the CLSYs remains unknown. Here, we identified a conserved CYC-YPMF motif that is specific to Pol IV and is positioned on the complex exterior. Furthermore, we found that this motif is essential for the co-purification of all four CLSYs with Pol IV, but that only one CLSY is present in any given Pol IV complex. These findings support a "one CLSY per Pol IV" model where the CYC-YPMF motif acts as a CLSY-docking site. Indeed, mutations in and around this motif phenocopy pol iv null and clsy quadruple mutants. Together, these findings provide structural and functional insights into a critical protein feature that distinguishes Pol IV from other RNA polymerases, allowing it to promote genome stability by targeting TEs for silencing.
Mots clés
DNA Transposable Elements, genetics, Arabidopsis Proteins, metabolism, DNA-Directed RNA Polymerases, metabolism, Gene Silencing, Arabidopsis, genetics, RNA, Small Interfering, metabolism, Gene Expression Regulation, Plant, RNA Polymerase II, metabolism, Protein Binding, Protein Domains, Conserved Sequence
Référence
Nat Commun. 2024 11 27;15(1):10298
