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Updated: Jun 25, 2026

In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles
Published on: August 25, 2022
Stability of artificial oil bodies constituted with recombinant caleosins
Ting-hang Liu1, Chia-lin Chyan, Feng-yin Li
1Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung, Taiwan
Abstract:
Caleosin is a unique calcium binding protein anchoring to the surface of seed oil bodies by its central hydrophobic domain composed of an amphiphatic alpha-helix and a proline-knot subdomain. Stable artificial oil bodies were successfully constituted with recombinant caleosin overexpressed in Escherichia coli. The stability of artificial oil bodies was slightly or severely reduced when the amphiphatic alpha-helix or proline-knot subdomain in the hydrophobic domain of caleosin was truncated. Deletion of the entire central hydrophobic domain substantially increased the solubility of the recombinant caleosin, leading to a complete loss of its capability to stabilize these oil bodies. A recombinant protein engineered with the hydrophobic domain of caleosin replaced by that of oleosin, the abundant structural protein of seed oil bodies, could stabilize the artificial oil bodies, in terms of thermo- and structural stability, as effectively as caleosin or oleosin.
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