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hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorDIELEN, Anne-Sophie
hal.structure.identifierDepartamento de Produção Vegetal
dc.contributor.authorSASSAKI, Flavio Tetsuo
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorMICHON, Thierry
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMENARD, Guillaume
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorPAGNY, Gaelle
hal.structure.identifierDepartamento de Produção Vegetal
dc.contributor.authorKRAUSE-SAKATE, Renate
hal.structure.identifierInstituto de Biociências, Departamento de Genética
dc.contributor.authorMAIA, Ivan De Godoy
hal.structure.identifierGénétique Diversité et Ecophysiologie des Céréales [GDEC]
dc.contributor.authorBADAOUI, Saloua
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorLE GALL, Olivier
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorCANDRESSE, Thierry
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorGERMAN-RETANA, Sylvie
dc.date.issued2011
dc.identifier.issn1464-6722
dc.description.abstractEnIn 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 α5 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 α5 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 α5 subunit. Further experiments demonstrated that, in LMV-infected lettuce cells, α5 is partially relocalized to HcPro-containing infection-specific inclusions. Susceptibility analyses of Arabidopsis mutants, knocked out for each At-PAE gene encoding α5, showed that one (KO-pae1) of the two mutants exhibited a significantly increased susceptibility to LMV infection. Taken together, these results extend to A. thalianaα5 the range of HcPro-interacting proteasomal subunits, and suggest that HcPro may modulate its associated RNase activity which may contribute to an antiviral response.
dc.language.isoen
dc.publisherWiley
dc.subjectVIROLOGIE
dc.subjectGENETIQUE
dc.subjectALPHA 5
dc.subjectRESISTANCE
dc.subjectACTIVITE RNASIQUE
dc.subjectBIFC
dc.subject 
dc.title.enThe 20S proteasome α5 subunit of Arabidopsis thaliana carries an RNase activity and interacts in planta with the Lettuce mosaic potyvirus HcPro protein
dc.typeArticle de revue
dc.identifier.doi10.1111/j.1364-3703.2010.00654.x
dc.subject.halSciences du Vivant [q-bio]/Sciences agricoles
bordeaux.journalMolecular Plant Pathology
bordeaux.page137-150
bordeaux.volume12
bordeaux.issue2
bordeaux.peerReviewedoui
hal.identifierhal-00964369
hal.version1
hal.popularnon
hal.audienceNon spécifiée
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-00964369v1
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