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J Biol Chem, Vol. 274, Issue 17, 11549-11556, April 23, 1999
From the Howard Hughes Medical Institute and Department of
Biochemistry, University of Texas Southwestern Medical Center,
Dallas, Texas 75235
We report here the reconstitution of the de
novo procaspase-9 activation pathway using highly purified
cytochrome c, recombinant APAF-1, and recombinant
procaspase-9. APAF-1 binds and hydrolyzes ATP or dATP to ADP or dADP,
respectively. The hydrolysis of ATP/dATP and the binding of cytochrome
c promote APAF-1 oligomerization, forming a large
multimeric APAF-1·cytochrome c complex. Such a complex
can be isolated using gel filtration chromatography and is by itself
sufficient to recruit and activate procaspase-9. The stoichiometric
ratio of procaspase-9 to APAF-1 is approximately 1 to 1 in the complex.
Once activated, caspase-9 disassociates from the complex and becomes
available to cleave and activate downstream caspases such as
caspase-3.
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