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Arabidopsis RNA processing body components LSM1 and DCP5 aid in the evasion of translational repression during Cauliflower mosaic virus infection
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).
Department of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden; Linnean Center for Plant Biology, Uppsala, Sweden.
Institut de Biologie Moléculaire des Plantes, CNRS, Université de Strasbourg, Strasbourg, France.
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2022 (Engelska)Ingår i: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 34, nr 8, s. 3128-3147Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Viral infections impose extraordinary RNA stress, triggering cellular RNA surveillance pathways such as RNA decapping, nonsense-mediated decay, and RNA silencing. Viruses need to maneuver among these pathways to establish infection and succeed in producing high amounts of viral proteins. Processing bodies (PBs) are integral to RNA triage in eukaryotic cells, with several distinct RNA quality control pathways converging for selective RNA regulation. In this study, we investigated the role of Arabidopsis thaliana PBs during Cauliflower mosaic virus (CaMV) infection. We found that several PB components are co-opted into viral factories that support virus multiplication. This pro-viral role was not associated with RNA decay pathways but instead, we established that PB components are helpers in viral RNA translation. While CaMV is normally resilient to RNA silencing, dysfunctions in PB components expose the virus to this pathway, which is similar to previous observations for transgenes. Transgenes, however, undergo RNA quality control-dependent RNA degradation and transcriptional silencing, whereas CaMV RNA remains stable but becomes translationally repressed through decreased ribosome association, revealing a unique dependence among PBs, RNA silencing, and translational repression. Together, our study shows that PB components are co-opted by the virus to maintain efficient translation, a mechanism not associated with canonical PB functions.

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Oxford University Press, 2022. Vol. 34, nr 8, s. 3128-3147
Nationell ämneskategori
Cellbiologi Biokemi och molekylärbiologi Botanik
Identifikatorer
URN: urn:nbn:se:umu:diva-198905DOI: 10.1093/plcell/koac132ISI: 000796682800001PubMedID: 35511183Scopus ID: 2-s2.0-85136044335OAI: oai:DiVA.org:umu-198905DiVA, id: diva2:1692906
Forskningsfinansiär
Vetenskapsrådet, 2017-05036Knut och Alice Wallenbergs Stiftelse, 2019-0062Bio4EnergyScience for Life Laboratory, SciLifeLabSwedish National Infrastructure for Computing (SNIC)VinnovaTillgänglig från: 2022-09-05 Skapad: 2022-09-05 Senast uppdaterad: 2022-09-05Bibliografiskt granskad

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Mahboubi, AmirHanson, Johannes

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CellbiologiBiokemi och molekylärbiologiBotanik

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