Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies.
Oleosin, a unique structural protein anchoring onto the surface of seed oil bodies by its central hydrophobic domain, stabilizes these lipid-storage organelles as discrete entities. Stable artificial oil bodies have been successfully constituted with native or recombinant oleosins. In this study, recombinant sesame oleosin with 12 residues stepwise truncated from its central hydrophobic domain of 72 residues was overexpressed in Escherichia coli, was purified to homogeneity, and was used for the constitution. Artificial oil bodies constituted by truncated oleosins with the central hydrophobic domain longer than 36 residues were as stable as native sesame oil bodies, and those constituted by truncated oleosins lacking more than half of the original central hydrophobic domain inclined to coalesce upon collision or aggregation.
Peng
Chi-Chung
CC
Department of Biotechnology, National Formosa University, Yunlin, Taiwan.
Lee
Viola S Y
VS
Lin
Meei-Yn
MY
Huang
Hsin-Yi
HY
Tzen
Jason T C
JT
D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D057927:Hydrophobic and Hydrophilic Interactions; D015388:Organelles / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics*; D015202:Protein Engineering; D011994:Recombinant Proteins; D012639:Seeds / Q000648:ultrastructure*
D010940:Plant Proteins; D011994:Recombinant Proteins; C110161:oleosin protein, Sesamum indicum