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Research article - Peer-reviewed, 2022

Arabidopsis RNA processing body components LSM1 and DCP5 aid in the evasion of translational repression during Cauliflower mosaic virus infection

Hoffmann, Gesa; Mahboubi, Amir; Bente, Heinrich; Garcia, Damien; Hanson, Johannes; Hafren, Anders;

Abstract

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.Arabidopsis RNA processing body components LSM1 and DCP5 are co-opted by Cauliflower mosaic virus to maintain efficient virus translation in the presence of RNA DEPENDENT POLYMERASE6-governed silencing.

Published in

Plant Cell

2022, volume: 34, number: 8, pages: 3128-3147
Publisher: OXFORD UNIV PRESS INC

Authors' information

Swedish University of Agricultural Sciences, Department of Plant Biology
Mahboubi, Amir
Umea University
Bente, Heinrich
Swedish University of Agricultural Sciences, Department of Plant Biology
Garcia, Damien
Universites de Strasbourg Etablissements Associes
Hanson, Johannes
Umea University
Swedish University of Agricultural Sciences, Department of Plant Biology

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication Identifiers

DOI: https://doi.org/10.1093/plcell/koac132

URI (permanent link to this page)

https://res.slu.se/id/publ/117340