Jang, Geng-Jen, Payne-Dwyer, Alex orcid.org/0000-0001-8802-352X, Maple, Robert et al. (7 more authors) (Accepted: 2025) In vivo properties of Arabidopsis FCA condensates involved in RNA 3’ processing. EMBO Journal. ISSN 0261-4189 (In Press)
Abstract
Our understanding of the functional requirements underpinning biomolecular condensation in vivo is still relatively poor. The Arabidopsis RNA binding protein FCA is found in liquid-like nuclear condensates that function in transcription termination, promoting proximal polyadenylation at many targets in the Arabidopsis genome. To further understand the properties of these condensates in vivo we used single particle tracking experiments on FCA reporters stably expressed at endogenous levels in plant nuclei. These revealed FCA forms a core oligomer of ~4 molecules that multimerizes into higher-order particles. This assembles into macromolecular condensates through the function of the coiled-coil protein FLL2, which is genetically required for FCA function. FLL2 predominately co25 localizes with FCA in larger sized condensates. A missense mutation in the FCA RRM domain, also genetically required for FCA function, reduced both average FCA particle and condensate size but did not perturb the core oligomer. Our work points to a modular structure for FCA condensates involving multimerization of core oligomers that assemble into functional macromolecular condensates via associated RNA and FLL2 interactions.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | This is an author-produced version of the published paper. Uploaded in accordance with the University’s Research Publications and Open Access policy. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) The University of York > Faculty of Sciences (York) > Physics (York) |
Depositing User: | Pure (York) |
Date Deposited: | 21 Feb 2025 12:30 |
Last Modified: | 21 Feb 2025 12:50 |
Status: | In Press |
Refereed: | Yes |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:223654 |
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