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Structural characterization of HC-Pro, a plant virus multifunctional protein.

hal.structure.identifierInteractions cellulaires et moléculaires [ICM]
dc.contributor.authorPLISSON, Célia
dc.contributor.authorDRUCKER, M.
hal.structure.identifierBiologie Intégrative et Virologie des Insectes [Univ. de Montpellier II] [BIVI]
dc.contributor.authorBLANC, Stéphane
hal.structure.identifierGénomique, développement et pouvoir pathogène [GD2P]
dc.contributor.authorGERMAN-RETANA, Sylvie
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorLE GALL, Olivier
hal.structure.identifierInteractions cellulaires et moléculaires [ICM]
dc.contributor.authorTHOMAS, Daniel
hal.structure.identifierInteractions cellulaires et moléculaires [ICM]
dc.contributor.authorBRON, Patrick
dc.date.accessioned2025-02-12T03:07:45Z
dc.date.available2025-02-12T03:07:45Z
dc.date.issued2003
dc.identifier.issn0021-9258
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/204807
dc.description.abstractEnThe helper component proteinase (HC-Pro) is a key protein encoded by plant viruses of the genus Potyvirus. HC-Pro is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of post-transcriptional gene silencing. Structural knowledge of HC-Pro is required to better understand its multiple functions. To this aim, we purified His-tagged wild-type HC-Pro and a N-terminal deletion mutant (DeltaHC-Pro) from plants infected with recombinant potyviruses. Biochemical analysis of the recombinant proteins confirmed that HC-Pro is a dimer in solution, that the N terminus is not essential for self-interaction, and that a large C-terminal domain is highly resistant to proteolysis. Two-dimensional crystals of the recombinant proteins were successfully grown on Ni2+-chelating lipid monolayers. Comparison of projection maps of negatively stained crystals revealed that HC-Pro is composed of two domains separated by a flexible constriction. Cryo-electron crystallography of DeltaHC-Pro allowed us to calculate a projection map at 9-A resolution. Our data from electron microscopy, biochemical analysis, and secondary structure predictions lead us to suggest a model for structure/function relationships in the HC-Pro protein
dc.language.isoen
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dc.rights.urihttp://creativecommons.org/licenses/by-nc/
dc.subjectVIROLOGIE
dc.subject.enHC-PRO
dc.subject.enCARACTERISATION STRUCURALE
dc.title.enStructural characterization of HC-Pro, a plant virus multifunctional protein.
dc.typeArticle de revue
dc.identifier.doi10.1074/jbc.M302512200
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
bordeaux.journalJournal of Biological Chemistry
bordeaux.page23761
bordeaux.volume278
bordeaux.hal.laboratoriesBiologie du Fruit & Pathologie (BFP) - UMR 1332*
bordeaux.issue26
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionINRAE
bordeaux.peerReviewedoui
hal.identifierhal-00108282
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-00108282v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20Biological%20Chemistry&rft.date=2003&rft.volume=278&rft.issue=26&rft.spage=23761&rft.epage=23761&rft.eissn=0021-9258&rft.issn=0021-9258&rft.au=PLISSON,%20C%C3%A9lia&DRUCKER,%20M.&BLANC,%20St%C3%A9phane&GERMAN-RETANA,%20Sylvie&LE%20GALL,%20Olivier&rft.genre=article


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