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Hydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBARRA, Amandine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorDOUBLET, Bénédicte
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCERÉ, Nicolas
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierUniversity of Sydney
dc.contributor.authorCHARON, Justine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
dc.date.issued2019
dc.identifier.issn1661-6596
dc.description.abstractEnProtein intrinsic disorder is involved in many biological processes and good experimental models are valuable to investigate its functions. The potyvirus genome-linked protein, VPg, displays many features of an intrinsically disordered protein. The virus cycle requires the formation of a complex between VPg and eIF4E, one of the host translation initiation factors. An in-depth characterization of the hydrodynamic properties of VPg, eIF4E, and of their binary complex VPg-eIF4E was carried out. Two complementary experimental approaches, size-exclusion chromatography and fluorescence anisotropy, which is more resolving and revealed especially suitable when protein concentration is the limiting factor, allowed to estimate monomers compaction upon complex formation. VPg possesses a high degree of hydration which is in agreement with its classification as a partially folded protein in between a molten and pre-molten globule. The natively disordered first 46 amino acids of eIF4E contribute to modulate the protein hydrodynamic properties. The addition of an N-ter His tag decreased the conformational entropy of this intrinsically disordered region. A comparative study between the two tagged and untagged proteins revealed the His tag contribution to proteins hydrodynamic behavior.
dc.language.isoen
dc.publisherMDPI
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subjectplant virus
dc.subjectmolten globule
dc.subjectprotein-protein interaction
dc.subjectfluorescence anisotropy
dc.subjectprotein hydrodynamics
dc.subject.enintrinsically disordered protein
dc.subject.eneIF4E
dc.subject.enVPg
dc.subject.enpotyvirus
dc.title.enHydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex
dc.typeArticle de revue
dc.identifier.doi10.3390/ijms20071794
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
bordeaux.journalInternational Journal of Molecular Sciences
bordeaux.page1794
bordeaux.volume20
bordeaux.issue7
bordeaux.peerReviewedoui
hal.identifierhal-02623838
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02623838v1
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