High water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed lipid bodies
2011
Gohon, Yann | Vindigni, Jean-David, J.-D. | Pallier, Agnes, A. | Wien, Franck, F. | Celia, Hervé, H. | Giuliani, Alexandre, A. | Tribet, Christophe, C. | Chardot, Thierry, T. | Briozzo, Pierre, P. | Institut Jean-Pierre Bourgin (IJPB) ; Institut National de la Recherche Agronomique (INRA)-AgroParisTech | Laboratoire de Physico-Chimie des Polymères et des Milieux Dispersés (PPMD) ; Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris) ; Université Paris Sciences et Lettres (PSL)-Université Paris Sciences et Lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS) | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM) ; Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) | Département Caractérisation et Elaboration des Produits Issus de l'Agriculture (CEPIA) ; Institut National de la Recherche Agronomique (INRA)
Seed lipid bodies constitute natural emulsions stabilized by specialized integral membrane proteins, among which the most abundant are oleosins, followed by the calcium binding caleosin. These proteins exhibit a triblock structure, with a highly hydrophobic central region comprising up to 71 residues. Little is known on their three-dimensional structure. Here we report the solubilization of caleosin and of two oleosins in aqueous solution, using various detergents or original amphiphilic polymers, amphipols. All three proteins, insoluble in water buffers, were maintained soluble either by anionic detergents or amphipols. Neutral detergents were ineffective. In complex with amphipols the oleosins and caleosin contain more beta and less alpha secondary structures than in the SDS detergent, as evaluated by synchrotron radiation circular dichroism. These are the first reported structural results on lipid bodies proteins maintained in solution with amphipols, a promising alternative to notoriously denaturing detergents. (c) 2010 Elsevier B.V. All rights reserved.
Show more [+] Less [-]Bibliographic information
This bibliographic record has been provided by Institut national de la recherche agronomique