ALBA proteins facilitate cytoplasmic YTHDF-mediated reading of m6A in Arabidopsis

N6-methyladenosine (m6A) exerts many of its regulatory effects on eukaryotic mRNAs by recruiting cytoplasmic YT521-B homology-domain family (YTHDF) proteins. Here, we show that in Arabidopsis thaliana, the interaction between m6A and the major YTHDF protein ECT2 also involves the mRNA-binding ALBA p...

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Detalles Bibliográficos
Autores: Reichel, Marlene, Tankmar, Mathias Due, Rennie, Sarah, Arribas-Hernández, Laura, Lewinski, Martin, Köster, Tino, Wang, Naiqi, Millar, Anthony A., Staiger, Dorothee, Brodersen, Peter
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/378959
Acceso en línea:http://hdl.handle.net/10261/378959
https://api.elsevier.com/content/abstract/scopus_id/85210556182
Access Level:acceso abierto
Palabra clave:ALBA Proteins
ECT2
Intrinsically Disordered Regions (IDR)
N6-Methyladenosine (m6A)
YTHDF Proteins
Descripción
Sumario:N6-methyladenosine (m6A) exerts many of its regulatory effects on eukaryotic mRNAs by recruiting cytoplasmic YT521-B homology-domain family (YTHDF) proteins. Here, we show that in Arabidopsis thaliana, the interaction between m6A and the major YTHDF protein ECT2 also involves the mRNA-binding ALBA protein family. ALBA and YTHDF proteins physically associate via a deeply conserved short linear motif in the intrinsically disordered region of YTHDF proteins and their mRNA target sets overlap, with ALBA4 binding sites being juxtaposed to m6A sites. These binding sites correspond to pyrimidine-rich elements previously found to be important for m6A binding to ECT2. Accordingly, both the biological functions of ECT2, and its binding to m6A targets in vivo, require ALBA association. Our results introduce the YTHDF-ALBA complex as the functional cytoplasmic m6A-reader in Arabidopsis, and define a molecular foundation for the concept of facilitated m6A reading, which increases the potential for combinatorial control of