Fold of an oleosin targeted to cellular oil bodies
| Autor: | Jean-David Vindigni, Yann Gohon, Zoi Erpapazoglou, Alexandre Giuliani, Franjo Jagic, Frank Wien, Roselyne Tache, Marine Froissard, Thierry Chardot |
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| Přispěvatelé: | Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Département Caractérisation et Elaboration des Produits Issus de l'Agriculture, Institut National de la Recherche Agronomique (INRA), Inst Biol Physicochim Biol Cellulaire & Mol Eucar, Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Předmět: |
0106 biological sciences
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences Circular dichroism Protein Folding Oleosin Arabidopsis SUNFLOWER 01 natural sciences Biochemistry Protein Structure Secondary Foscholine 12 Oil body Protein structure Protein fold Protein secondary structure Integral membrane protein 0303 health sciences Circular Dichroism PERILIPIN-A Protein folding BODY PROTEINS Hydrophobic and Hydrophilic Interactions CIRCULAR-DICHROISM SPECTROSCOPY Phosphorylcholine Recombinant Fusion Proteins Green Fluorescent Proteins Immunoblotting Biophysics Saccharomyces cerevisiae Biology 03 medical and health sciences PROTEIN SECONDARY STRUCTURE 030304 developmental biology Arabidopsis Proteins CENTRAL HYDROPHOBIC DOMAIN LIPDROPLETS Cell Membrane Membrane Proteins Cell Biology IN-VITRO SRCD Microscopy Fluorescence ARABIDOPSIS-THALIANA Heterologous expression Oils Alpha helix 010606 plant biology & botany |
| Zdroj: | Biochimica et Biophysica Acta:Biomembranes Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2013, 1828 (8), pp.1881-1888. ⟨10.1016/j.bbamem.2013.04.009⟩ |
| ISSN: | 0005-2736 1879-2642 |
| DOI: | 10.1016/j.bbamem.2013.04.009 |
| Popis: | In cells, from bacteria to plants or mammals, lipids are stored in natural emulsions called oil bodies (OBs). This organelle is surrounded by a phospholipid monolayer which is thought to contain integral proteins involved in its stabilization. The insertion and fold of these proteins into the phospholipid monolayer are poorly understood. In seed OBs, the most abundant integral proteins are oleosins, which contain a 70-residue central hydrophobic domain. The secondary structure of solubilized oleosins varies greatly from mainly alpha helices to a predominantly beta sheets depending on the detergent used. To study the fold of integral membrane proteins inserted in a cellular OB environment, S3 protein, the major Arabidopsis thaliana seed oleosin, was targeted to Saccharomyces cerevisiae OBs. The diameter of purified yeast OBs harboring S3 or S3 fused with the Green Fluorescent Protein (GFP) was smaller and more homogeneous than plant OBs. Comparison of the secondary structure of S3 and S3-GFP was used to validate the structure of folded S3. Circular dichroism using synchrotron radiation indicated that S3 and S3-GFP in yeast OBs contain mainly beta secondary structures. While yeast OBs are chemically different to A. thaliana seed OBs, this approach allowed the secondary structure of S3 in OB particles to be determined for the first time. (C) 2013 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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