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[Preprint]. 2024 Sep 29:2023.07.11.548587. Originally published 2023 Jul 11. [Version 2] doi: 10.1101/2023.07.11.548587

Figure 1: Validation of the split-luciferase based extraction assay.

Figure 1:

A) Diagram for split-luciferase extraction assay. Note that for properly reconstituted liposomes, both the HiBiT and thrombin sites are in the lumen of the proteoliposome.

B) Workflow for split-luciferase assay.

C) Protease protection assay shows that substrates are properly oriented. Anti-HiBiT western blot of pre-cleared liposomes shows minimal loss of signal upon addition of thrombin protease, but complete loss of signal with both thrombin and detergent.

D) Addition of an inert His6-tagged protein to ultracentrifugation improves liposome pelleting efficiency and reduces background activity.

E) Standard curves used to calculate percent substrate extracted. Four separate reconstitutions of the standard Sumo-Sec22 model substrate in standard liposomes show a linear and reproducible signal. Different concentrations of pre-cleared, but unreacted proteoliposomes were mixed with LgBiT and furimazine reagent in detergent, which permeablizes the proteoliposomes. The X-axis refers to the percent of substrate in the extraction assay.

F) The split-luciferase extraction assay shows ATP-dependent and physiological substrate extraction activity. The known substrate Sec22 is extracted whereas the native mitochondrial protein Fis1 is not extracted unless a hydrophobic patch is added, which serves as an Msp1 recognition sequence. Error bars show standard error of the mean.