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• W1985168538 endingPage "1888" @default.
• W1985168538 startingPage "1881" @default.
• W1985168538 abstract "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." @default.
• W1985168538 created "2016-06-24" @default.
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• W1985168538 date "2013-08-01" @default.
• W1985168538 modified "2023-09-30" @default.
• W1985168538 title "Fold of an oleosin targeted to cellular oil bodies" @default.
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• W1985168538 doi "https://doi.org/10.1016/j.bbamem.2013.04.009" @default.
• W1985168538 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23603223" @default.
• W1985168538 hasPublicationYear "2013" @default.
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