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J Biol Chem, Vol. 274, Issue 30, 20759-20762, July 23, 1999
From the Division of Tumor Immunology, Dana-Farber Cancer Institute
and Department of Medicine, Harvard Medical School,
Boston, Massachusetts 02115
DNA fragmentation factor (DFF) functions
downstream of caspase-3 and directly triggers DNA fragmentation during
apoptosis. Here we described the identification and characterization of
DFF35, an isoform of DFF45 comprised of 268 amino acids. Functional
assays have shown that only DFF45, not DFF35, can assist in the
synthesis of highly active DFF40. Using the deletion mutants, we mapped the function domains of DFF35/45 and demonstrated that the intact structure/conformation of DFF45 is essential for it to function as a
chaperone and assist in the synthesis of active DFF40. Whereas the
amino acid residues 101-180 of DFF35/45 mediate its binding to DFF40,
the amino acid residues 23-100, which is homologous between DFF35/45
and DFF40, may function to inhibit the activity of DFF40. In contrast
to DFF45, DFF35 cannot work as a chaperone, but it can bind to DFF40
more strongly than DFF45 and can inhibit its nuclease activity. These
findings suggest that DFF35 may function in vivo as an
important alternative mechanism to inhibit the activity of DFF40 and
further, that the inhibitory effects of both DFF35 and DFF45 on DFF40
can put the death machinery under strict control.
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