Redox sensitive protein droplets from recombinant oleosin.

ABSTRACT: Protein engineering enables the creation of materials with designer functionality and tailored responsiveness. Here, we design a protein with two control motifs for its phase separation into micron sized liquid droplets - one driven by a hydrophobic domain and the other by oxidation of a disulfide bond. Our work is based on the plant surfactant protein, oleosin, which has a hydrophobic domain but no cysteines. Oleosin phase separates to form liquid droplets below a critical temperature akin to many naturally occurring membrane-less organelles. Sequence mutations are made to introduce a cysteine residue into oleosin. The addition of a cysteine causes phase separation at a lower concentration and increases the phase transition temperature. Adding a reducing agent to phase-separated, cysteine

SUBMITTER: Reed EH 

PROVIDER: S-EPMC6502463 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature