Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation
| العنوان: | Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation |
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| المؤلفون: | Alexandre Giuliani, Véronique Solé-Jamault, Denis Renard, Adeline Boire, Line Sahli |
| المساهمون: | Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Département Caractérisation et Elaboration des Produits Issus de l'Agriculture (CEPIA), DISCO, Partenaires INRAE, regional programme 'Food for Tomorrow/Cap Aliment, Research, Education and Innovation in Pays de la Loire' - French Region Pays de la Loire, European Regional Development Fund (FEDER)European Union (EU), Sahli, Line |
| المصدر: | Scientific Reports Scientific Reports, Nature Publishing Group, 2019, 9, ⟨10.1038/s41598-019-49745-2⟩ Scientific Reports (9), . (2019) Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019) |
| بيانات النشر: | Springer Science and Business Media LLC, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Models, Molecular, 0301 basic medicine, Phase transition, Protein Conformation, Liquid-Liquid Extraction, Static Electricity, lcsh:Medicine, Gliadin, Phase Transition, Article, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Static electricity, Storage protein, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, lcsh:Science, Triticum, 2. Zero hunger, chemistry.chemical_classification, Intrinsically disordered proteins, Multidisciplinary, Aqueous solution, Ethanol, Chemistry, Hydrogen bond, lcsh:R, Proteins, nutritional and metabolic diseases, food and beverages, digestive system diseases, 030104 developmental biology, Ionic strength, Seeds, Biophysics, lcsh:Q, 030217 neurology & neurosurgery |
| الوصف: | Wheat storage proteins, gliadins, were found to form in vitro condensates in 55% ethanol/water mixture by decreasing temperature. The possible role of this liquid-liquid phase separation (LLPS) process on the in vivo gliadins storage is elusive and remains to be explored. Here we use γ-gliadin as a model of wheat proteins to probe gliadins behavior in conditions near physiological conditions. Bioinformatic analyses suggest that γ-gliadin is a hybrid protein with N-terminal domain predicted to be disordered and C-terminal domain predicted to be ordered. Spectroscopic data highlight the disordered nature of γ-gliadin. We developed an in vitro approach consisting to first solubilize γ-gliadin in 55% ethanol (v/v) and to progressively decrease ethanol ratio in favor of increased aqueous solution. Our results show the ability of γ-gliadin to self-assemble into dynamic droplets through LLPS, with saturation concentrations ranging from 25.9 µM ± 0.85 µM (35% ethanol (v/v)) to 3.8 µM ± 0.1 µM (0% ethanol (v/v)). We demonstrate the importance of the predicted ordered C-terminal domain of γ-gliadin in the LLPS by highlighting the protein condensates transition from a liquid to a solid state under reducing conditions. We demonstrate by increasing ionic strength the role displayed by electrostatic interactions in the phase separation. We also show the importance of hydrogen bonds in this process. Finally, we discuss the importance of gliadins condensates in their accumulation and storage in the wheat seed. |
| وصف الملف: | application/pdf |
| تدمد: | 2045-2322 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60c7601f16e2ee119bc80edb6fe27ad1 https://doi.org/10.1038/s41598-019-49745-2 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....60c7601f16e2ee119bc80edb6fe27ad1 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20452322 |
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