Stability of artificial oil bodies constituted with recombinant caleosins.
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.
Liu
Ting-hang
TH
Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung, Taiwan
Chyan
Chia-lin
CL
Li
Feng-yin
FY
Tzen
Jason T C
JT
D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D004355:Drug Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D015388:Organelles / Q000737:chemistry*; D010938:Plant Oils / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry*; D012995:Solubility
D002135:Calcium-Binding Proteins; D010938:Plant Oils; D010940:Plant Proteins; D011994:Recombinant Proteins; C402836:caleosin protein, Sesamum indicum