Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4.

摘要: Abstract Programmed cell death in Caenorhabditis elegans is initiated by the binding of EGL-1 to CED-9, which disrupts CED-4/CED-9 complex and allows CED-4 activate cell-killing caspase CED-3. Here we demonstrate that C-terminal half necessary sufficient for CED-9 killing cells. Structure EGL-1/CED-9 revealed adopts an extended α-helical conformation induces substantial structural rearrangements upon binding. interface mutants failed bind or release from complex, were unable induce vivo. A surface patch on different required EGL-1, was identified be responsible CED-4. These data suggest a working mechanism provide mechanistic framework understanding apoptosis activation C. .