6f08364dc15d3f939d9da8ee79b767be NucAciRes_a2024v52n14p8466.pdf 15da327ba253ec4c43b3c4bba9535ee744dd5e92 NucAciRes_a2024v52n14p8466.pdf 882b91a2ae125043b4ccd7094a2aad42aa917fce61ccb0494375182df111e279 NucAciRes_a2024v52n14p8466.pdf Title: Arabidopsis AGO1 N-terminal extension acts as an essential hub for PRMT5 interaction and post-translational modifications Subject: DOI: 10.1093/nar/gkae387 , 52, 14, 20-5-2024. Abstract: Plant ARGONAUTE (AGO) proteins play pivotal roles regulating gene expression through small  RNA (sRNA) -guided mechanisms. Among the 10 AGO proteins in Arabidopsis thaliana, AGO1 stands out as the main effector of post-transcriptional gene silencing. Intriguingly, a specific region of AGO1, its N-terminal extension (NTE), has garnered attention in recent studies due to its involvement in diverse regulatory functions, including subcellular localization, sRNA loading and interactions with regulatory factors. In the field of post-translational modifications (PTMs), little is known about arginine methylation in Arabidopsis AGOs. In this study, we show that NTE of AGO1 (NTEAGO1) undergoes symmetric arginine dimethylation at specific residues. Moreover, NTEAGO1 interacts with the methyltransferase PRMT5, which catalyzes its methylation. Notably, we observed that the lack of symmetric dimethylarginine has no discernible impact on AGO1’s subcellular localization or miRNA loading capabilities. However, the absence of PRMT5 significantly alters the loading of a subgroup of sRNAs into AGO1 and reshapes the NTEAGO1 interactome. Importantly, our research shows that symmetric arginine dimethylation of NTEs is a common process among Arabidopsis AGOs, with AGO1, AGO2, AGO3 and AGO5 undergoing this PTM. Overall, this work deepens our understanding of PTMs in the intricate landscape of RNA-associated gene regulation. Keywords: Author: Martn-Merchn Andrea, Lavatelli Antonela, Engler Camila, Gonzlez-Miguel VctorM., Moro Beln, Rosano GermnL., Bologna NicolasG. Creator: OUP Producer: Acrobat Distiller 24.0 (Windows); modified using iTextSharp 5.5.10 ©2000-2016 iText Group NV (AGPL-version) CreationDate: Mon Aug 5 08:17:14 2024 CEST ModDate: Mon Jun 16 18:45:53 2025 CEST Custom Metadata: yes Metadata Stream: yes Tagged: yes UserProperties: no Suspects: no Form: none JavaScript: no Pages: 17 Encrypted: no Page size: 612 x 792 pts (letter) Page rot: 0 File size: 2907426 bytes Optimized: no PDF version: 1.4 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- JDJFEL+dummy-space Type 1C WinAnsi yes yes no 82 0 JDJGEM+UniversLTStd-LightObl Type 1C Custom yes yes yes 181 0 JDJGEL+UniversLTStd-Light Type 1C Custom yes yes yes 182 0 JDJFMN+CMSY10 Type 1C Custom yes yes yes 1411 0 JDJFEP+UniversLTStd-BoldCn Type 1C Custom yes yes yes 1412 0 JDJHFH+RMTMI Type 1C Custom yes yes yes 81 0 JDJFEN+UniversLTStd-Cn Type 1C Custom yes yes yes 1413 0 JDJFEM+UniversLTStd-CnObl Type 1C Custom yes yes yes 1414 0 JDJHFG+SabonLTStd-Bold Type 1C Custom yes yes yes 519 0 JDJFDK+SabonLTStd-Roman Type 1C Custom yes yes yes 83 0 OAMPBH+ArialMT TrueType WinAnsi yes yes no 1 0 JDJFEO+UniversLTStd-Bold Type 1C Custom yes yes yes 84 0 JDJICF+SabonLTStd-Italic Type 1C Custom yes yes yes 78 0 JDJHFJ+UniversLTStd Type 1C Custom yes yes yes 79 0 JDJHFI+UniversLTStd-Obl Type 1C Custom yes yes yes 80 0 JDJIGG+EURM10 Type 1C Custom yes yes yes 127 0 JDJIEG+MTSY Type 1C Custom yes yes yes 128 0 JDJMOL+EURM7 Type 1C Custom yes yes yes 237 0 Jhove (Rel. 1.28.0, 2023-05-18) Date: 2025-06-17 02:46:28 CEST RepresentationInformation: NucAciRes_a2024v52n14p8466.pdf ReportingModule: PDF-hul, Rel. 1.12.4 (2023-03-16) LastModified: 2025-06-16 20:02:08 CEST Size: 2907426 Format: PDF Version: 1.4 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf Profile: Tagged PDF PDFMetadata: Objects: 1785 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: ViewerPreferences: HideToolbar: false HideMenubar: false HideWindowUI: false FitWindow: false CenterWindow: false DisplayDocTitle: true NonFullScreenPageMode: UseNone Direction: L2R ViewArea: CropBox ViewClip: CropBox PrintArea: CropBox PageClip: CropBox PageLayout: OneColumn PageMode: UseThumbs Language: English Outlines: Item: Title: Graphical abstract Destination: section.2.2.0 Item: Title: Introduction Destination: section.3.3.0 Item: Title: Materials and methods Destination: section.4.4.0 Item: Title: Results Destination: section.5.19.0 Item: Title: Discussion Destination: section.6.27.0 Item: Title: Data availability Destination: section.7.32.0 Item: Title: Supplementary data Destination: section.8.33.0 Item: Title: Acknowledgements Destination: section.9.34.0 Item: Title: Funding Destination: section.10.35.0 Item: Title: Conflict of interest statement Destination: section.11.36.0 Item: Title: References Destination: section.12.36.0 Info: Title: Arabidopsis AGO1 N-terminal extension acts as an essential hub for PRMT5 interaction and post-translational modifications Author: Martn-Merchn Andrea, Lavatelli Antonela, Engler Camila, Gonzlez-Miguel VctorM., Moro Beln, Rosano GermnL., Bologna NicolasG. Subject: DOI: 10.1093/nar/gkae387 , 52, 14, 20-5-2024. Abstract: Plant ARGONAUTE (AGO) proteins play pivotal roles regulating gene expression through small  RNA (sRNA) -guided mechanisms. Among the 10 AGO proteins in Arabidopsis thaliana, AGO1 stands out as the main effector of post-transcriptional gene silencing. Intriguingly, a specific region of AGO1, its N-terminal extension (NTE), has garnered attention in recent studies due to its involvement in diverse regulatory functions, including subcellular localization, sRNA loading and interactions with regulatory factors. In the field of post-translational modifications (PTMs), little is known about arginine methylation in Arabidopsis AGOs. In this study, we show that NTE of AGO1 (NTEAGO1) undergoes symmetric arginine dimethylation at specific residues. Moreover, NTEAGO1 interacts with the methyltransferase PRMT5, which catalyzes its methylation. Notably, we observed that the lack of symmetric dimethylarginine has no discernible impact on AGO1’s subcellular localization or miRNA loading capabilities. However, the absence of PRMT5 significantly alters the loading of a subgroup of sRNAs into AGO1 and reshapes the NTEAGO1 interactome. Importantly, our research shows that symmetric arginine dimethylation of NTEs is a common process among Arabidopsis AGOs, with AGO1, AGO2, AGO3 and AGO5 undergoing this PTM. Overall, this work deepens our understanding of PTMs in the intricate landscape of RNA-associated gene regulation. 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