ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding

The m A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m A readers constitute a super family of proteins with hu...

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Veröffentlicht in:RNA biology 2024-12, Vol.21 (1), p.1-958
Hauptverfasser: Seigneurin-Berny, Daphné, Karczewski, Claire, Delaforge, Elise, Yaacoub, Karen, Gaspar Litholdo, Jr, Celso, Favory, Jean-Jacques, Ringkjøbing Jensen, Malene, Bousquet-Antonelli, Cécile, Verdel, André
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container_end_page 958
container_issue 1
container_start_page 1
container_title RNA biology
container_volume 21
creator Seigneurin-Berny, Daphné
Karczewski, Claire
Delaforge, Elise
Yaacoub, Karen
Gaspar Litholdo, Jr, Celso
Favory, Jean-Jacques
Ringkjøbing Jensen, Malene
Bousquet-Antonelli, Cécile
Verdel, André
description The m A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved -Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA . Finally, we also identify small structural elements, located next to ECT2 YTH domain and conserved in a large set of YTH proteins, that enhance its binding to m A-methylated RNA. We propose from these findings that some of these regulatory regions are not limited to ECT2 or YTH readers of flowering plants but may be widespread among eukaryotic YTH readers.
doi_str_mv 10.1080/15476286.2024.2399914
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The main m A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved -Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA . 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subjects Adenosine - metabolism
Amino Acid Sequence
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Binding Sites
Intracellular Signaling Peptides and Proteins
Intrinsically Disordered Proteins - chemistry
Intrinsically Disordered Proteins - genetics
Intrinsically Disordered Proteins - metabolism
Life Sciences
Methylation
Protein Binding
Protein Domains
RNA, Plant - chemistry
RNA, Plant - genetics
RNA, Plant - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
title ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding
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