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Arabidopsis LSM1 and DCP5 proteins aid evasion of translational repression during Cauliflower Mosaic Virus infection

ABSTRACT: Arabidopsis LSM1 and DCP5 proteins aid evasion of translational repression during Cauliflower Mosaic Virus infection

PROVIDER: PRJNA799378 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17697100_1.fastq.gz	Fastqsanger.gz
	SRR17697100_2.fastq.gz	Fastqsanger.gz
	SRR17697101_1.fastq.gz	Fastqsanger.gz
	SRR17697101_2.fastq.gz	Fastqsanger.gz
	SRR17697102_1.fastq.gz	Fastqsanger.gz

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Arabidopsis LSM1 and DCP5 proteins aid evasion of translational repression during Cauliflower Mosaic Virus infection

Project description:Processing bodies are tightly connected with the RNA silencing machinery. Deletion of processing body components leads to succeptibility of Cauliflower Mosaic Virus to translational repression. Here, we investigated if this succeptibility is mediated through differential sRNA targeting of the viral genome.

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

Project description: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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