ArticleMolecular plant pathology2011
The 20S proteasome α5 subunit of Arabidopsis thaliana carries an RNase activity and interacts in planta with the lettuce mosaic potyvirus HcPro protein.
Article in Molecular plant pathology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 52 citations in OpenAlex.
- Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1-SlPA4 Interaction to Enhance Viral Infection.Molecular plant pathology · 2025Article
- Potyviral Helper-Component Protease: Multifaced Functions and Interactions with Host Proteins.Plants (Basel, Switzerland) · 2024Review
- Structural and functional characteristics and expression profile of the 20S proteasome gene family in Sorghum under abiotic stress.Frontiers in plant science · 2023Article
- Engineering Resistance Against Viruses in Field Crops Using CRISPR- Cas9.Current genomics · 2021Review
- Review
- Genome assembly and population genomic analysis provide insights into the evolution of modern sweet corn.Nature communications · 2021Article
- Article
- An E3 ubiquitin ligase from Nicotiana benthamiana targets the replicase of Bamboo mosaic virus and restricts its replication.Molecular plant pathology · 2019Article
- The HCPro from the Potyviridae family: an enviable multitasking Helper Component that every virus would like to have.Molecular plant pathology · 2018Review
- Plant immunity against viruses: antiviral immune receptors in focus.Annals of botany · 2017Review
- Proteome Profiling of Paulownia Seedlings Infected with Phytoplasma.Frontiers in plant science · 2017Article
- Plant Virus Infection and the Ubiquitin Proteasome Machinery: Arms Race along the Endoplasmic Reticulum.Viruses · 2016Review
- Tomato 26S Proteasome subunit RPT4a regulates ToLCNDV transcription and activates hypersensitive response in tomato.Scientific reports · 2016Article
- Article
- A procedure for the transient expression of genes by agroinfiltration above the permissive threshold to study temperature-sensitive processes in plant-pathogen interactions.Molecular plant pathology · 2014Article
- Intracellular coordination of potyviral RNA functions in infection.Frontiers in plant science · 2014Review
- The influence of cis-acting P1 protein and translational elements on the expression of Potato virus Y helper-component proteinase (HCPro) in heterologous systems and its suppression of silencing activity.Molecular plant pathology · 2013Article
- Ubiquitination during plant immune signaling.Plant physiology · 2012Review
- Interaction of the trans-frame potyvirus protein P3N-PIPO with host protein PCaP1 facilitates potyvirus movement.PLoS pathogens · 2012Article
- Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plants, the ubiquitin/26S proteasome system (UPS) plays a central role in protein degradation and is involved in many steps of defence mechanisms, regardless of the types of pathogen targeted. In addition to its proteolytic activities, the UPS ribonuclease (RNase) activity, previously detected in 20S proteasome preparations from cauliflower and sunflower (Helianthus annuus), has been shown to specifically target plant viral RNAs in vitro. In this study, we show that recombinant Arabidopsis thaliana proteasomal α(5) subunit expressed in Escherichia coli harbours an RNase activity that degrades Tobacco mosaic virus (TMV, Tobamovirus)- and Lettuce mosaic virus (LMV, Potyvirus)-derived RNAs in vitro. The analysis of mutated forms of the α(5) subunit demonstrated that mutation of a glutamic acid at position 110 affects RNase activity. Furthermore, it was demonstrated, using a bimolecular fluorescence complement assay, that the multifunctional helper component proteinase (HcPro) of LMV, already known to interfere with the 20S proteasome RNase activity in vitro, can interact in vivo with the recombinant α(5) subunit. Further experiments demonstrated that, in LMV-infected lettuce cells, α(5) is partially relocalized to HcPro-containing infection-specific inclusions. Susceptibility analyses of Arabidopsis mutants, knocked out for each At-PAE gene encoding α(5) , showed that one (KO-pae1) of the two mutants exhibited a significantly increased susceptibility to LMV infection. Taken together, these results extend to A. thaliana α(5) the range of HcPro-interacting proteasomal subunits, and suggest that HcPro may modulate its associated RNase activity which may contribute to an antiviral response.
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