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Article

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

UMR 1332 Biologie du Fruit et Pathologie, INRA, Université de Bordeaux, CS 20032, 33140 Villenave d’Ornon, France
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Present address: School of Life & Environmental Sciences, University of Sydney, Sydney, NSW 2006, Australia.
Int. J. Mol. Sci. 2019, 20(7), 1794; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20071794
Received: 13 March 2019 / Revised: 3 April 2019 / Accepted: 5 April 2019 / Published: 11 April 2019
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. View Full-Text
Keywords: intrinsically disordered protein; plant virus; eIF4E; VPg; potyvirus; molten globule; protein-protein interaction; fluorescence anisotropy; protein hydrodynamics intrinsically disordered protein; plant virus; eIF4E; VPg; potyvirus; molten globule; protein-protein interaction; fluorescence anisotropy; protein hydrodynamics
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MDPI and ACS Style

Walter, J.; Barra, A.; Doublet, B.; Céré, N.; Charon, J.; Michon, T. Hydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex. Int. J. Mol. Sci. 2019, 20, 1794. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20071794

AMA Style

Walter J, Barra A, Doublet B, Céré N, Charon J, Michon T. Hydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex. International Journal of Molecular Sciences. 2019; 20(7):1794. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20071794

Chicago/Turabian Style

Walter, Jocelyne, Amandine Barra, Bénédicte Doublet, Nicolas Céré, Justine Charon, and Thierry Michon. 2019. "Hydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex" International Journal of Molecular Sciences 20, no. 7: 1794. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20071794

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