Mechanistic Issues of the Interaction of the Hairpin-Forming Domain of tBid with Mitochondrial Cardiolipin
Figure 1
The helix αH6 targets tBid to the mitochondria.
(A) and (B) Computer-based analysis of the biophysical properties of Bid. (A) Kite & Doolittle profile of Bid (PROSTCALE, Swiss Institute of Bioinformatics). (B) Comparison of the isoelectric points (pI), hydrophobicities and charges of tBid, αH6 and αH6m. (C) Schematic representation of tBid-EYFP mutants. (D) and (E) CV-1 cells were transfected with plasmids endoding tBid-EYFP mutants in presence of 10 µM of Bok-D to inhibit caspases activation and subsequent cell death. 24 h later, cells were stained with 20 nM of the mitochondrial potential probe TMRE and the localization of the tBid-EYFP mutants was determined using confocal microscopy (D) and microspectrofluorometry analysis (E).