WALTER, Jocelyne; BARRA, Amandine; DOUBLET, Bénédicte; CERÉ, Nicolas; CHARON, Justine; MICHON, Thierry

doi:10.3390/ijms20071794

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WALTER, Jocelyne
Biologie du fruit et pathologie [BFP]

BARRA, Amandine
Biologie du fruit et pathologie [BFP]

DOUBLET, Bénédicte
Biologie du fruit et pathologie [BFP]

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Article de revue

Ce document a été publié dans

International Journal of Molecular Sciences. 2019, vol. 20, n° 7, p. 1794

MDPI

Résumé en anglais

Protein 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.< Réduire

Mots clés

plant virus

molten globule

protein-protein interaction

fluorescence anisotropy

protein hydrodynamics

Mots clés en anglais

intrinsically disordered protein

eIF4E

VPg

potyvirus