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Cauliflower mosaic virus protein P6 is a multivalent node for RNA granule proteins and interferes with stress granule responses during plant infection
Department of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden; Linnean Center for Plant Biology, Uppsala, Sweden.
Department of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden; Linnean Center for Plant Biology, Uppsala, Sweden.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik. Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå Plant Science Centre (UPSC).
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik. Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå Plant Science Centre (UPSC).ORCID-id: 0000-0002-5605-7984
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2023 (Engelska)Ingår i: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 35, nr 9, s. 3363-3382Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Biomolecular condensation is a multipurpose cellular process that viruses use ubiquitously during their multiplication. Cauliflower mosaic virus replication complexes are condensates that differ from those of most viruses, as they are nonmembranous assemblies that consist of RNA and protein, mainly the viral protein P6. Although these viral factories (VFs) were described half a century ago, with many observations that followed since, functional details of the condensation process and the properties and relevance of VFs have remained enigmatic. Here, we studied these issues in Arabidopsis thaliana and Nicotiana benthamiana. We observed a large dynamic mobility range of host proteins within VFs, while the viral matrix protein P6 is immobile, as it represents the central node of these condensates. We identified the stress granule (SG) nucleating factors G3BP7 and UBP1 family members as components of VFs. Similarly, as SG components localize to VFs during infection, ectopic P6 localizes to SGs and reduces their assembly after stress. Intriguingly, it appears that soluble rather than condensed P6 suppresses SG formation and mediates other essential P6 functions, suggesting that the increased condensation over the infection time-course may accompany a progressive shift in selected P6 functions. Together, this study highlights VFs as dynamic condensates and P6 as a complex modulator of SG responses.

Ort, förlag, år, upplaga, sidor
Oxford University Press, 2023. Vol. 35, nr 9, s. 3363-3382
Nationell ämneskategori
Cellbiologi Biokemi och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-214982DOI: 10.1093/plcell/koad101ISI: 000971386700001PubMedID: 37040611Scopus ID: 2-s2.0-85171990221OAI: oai:DiVA.org:umu-214982DiVA, id: diva2:1804686
Forskningsfinansiär
Vetenskapsrådet, 2017-05036Carl Tryggers stiftelse för vetenskaplig forskning , CTS 17:180Knut och Alice Wallenbergs Stiftelse, 2019-0062Bio4EnergyTillgänglig från: 2023-10-13 Skapad: 2023-10-13 Senast uppdaterad: 2023-10-13Bibliografiskt granskad

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Mahboubi, AmirHanson, Johannes

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Institutionen för fysiologisk botanikUmeå Plant Science Centre (UPSC)
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The Plant Cell
CellbiologiBiokemi och molekylärbiologi

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