ArticleInternational journal of molecular sciences2019
Hydrodynamic Behavior of the Intrinsically Disordered Potyvirus Protein VPg, of the Translation Initiation Factor eIF4E and of their Binary Complex.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 12 citations in OpenAlex.
- DNA binding and dimerization of the SOG1 NAC domain are functionally linked with its ability to undergo liquid-liquid phase separation.Nucleic acids research · 2026Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Phosphorylation of eukaryotic initiation factor eIFiso4E enhances the binding rates to VPg of turnip mosaic virus.PloS one · 2021Article
- Spectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E.International journal of molecular sciences · 2020Article
- Macromolecular Interactions of Disordered Proteins.International journal of molecular sciences · 2020Article
- Structural studies of the eIF4E-VPg complex reveal a direct competition for capped RNA: Implications for translation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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Abstract
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.
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