A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants

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N6-methyladenosine (m6A) in mRNA is key to eukaryotic gene regulation. Many m6A functions involve RNA-binding proteins that recognize m6A via a YT521-B Homology (YTH) domain. YTH domain proteins contain long intrinsically disordered regions (IDRs) that may mediate phase separation and interaction with protein partners, but whose precise biochemical functions remain largely unknown. The Arabidopsis thaliana YTH domain proteins ECT2, ECT3, and ECT4 accelerate organogenesis through stimulation of cell division in organ primordia. Here, we use ECT2 to reveal molecular underpinnings of this function. We show that stimulation of leaf formation requires the long N-terminal IDR, and we identify two short IDR elements required for ECT2-mediated organogenesis. Of these two, a 19-amino acid region containing a tyrosine-rich motif conserved in both plant and metazoan YTHDF proteins is necessary for binding to the major cytoplasmic poly(A)-binding proteins PAB2, PAB4, and PAB8. Remarkably, overexpression of PAB4 in leaf primordia partially rescues the delayed leaf formation in ect2 ect3 ect4 mutants, suggesting that the ECT2-PAB2/4/8 interaction on target mRNAs of organogenesis-related genes may overcome limiting PAB concentrations in primordial cells.
OriginalsprogEngelsk
Artikelnummere57741
TidsskriftEMBO Reports
Vol/bind24
Udgave nummer12
Antal sider19
ISSN1469-221X
DOI
StatusUdgivet - 2023

Bibliografisk note

Funding Information:
We thank Lena Bjørn Johansson, Daniel Tobias Kyndesen Lahti, Ida Thorøe Michler, Magnus von Holstein‐Rathlou, and Jakub Najbar for technical assistance. Theo Bölsterli, René Hvidberg Petersen, and their teams are thanked for plant care. Erwin Schoof and the proteomics platform at Denmark's Technical University are thanked for running protein identification by liquid chromatography‐mass spectrometry. Carlotta Porcelli is thanked for help with analysis of mass spectrometry data. Morten Nørholm is thanked for advice and help on conducting bacterial two‐hybrid analysis, and Michael Askvad Sørensen is thanked for the gift of MacConkey/sugar plates. Ida Marie Zobbe Sjøgaard is thanked for the kind gift of purified GST. Birthe B. Kragelund is thanked for sparring on IDP expression. This work was supported by a Hallas‐Møller Ascending Investigator Fellowship grant from Novo Nordisk Foundation (NNF19OC0054973), a Consolidator Grant from the European Research Council (PATHORISC, ERC‐2016‐CoG 726417), a Research Infrastructure Grant from Carlsberg Fondet (CF20‐0659), and an Instrument Grant from Brdr Hartmann Fonden (A35879), all to PB.

Publisher Copyright:
© 2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

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