Abstract:
:CAD/DFF40, the nuclease responsible for DNA fragmentation during apoptosis, exists as a heterodimeric complex with DFF45/ICAD. This study determines the molecular mechanisms of regulation of DFF40 via the chaperone and inhibition activities of DFF45. We analyze proteins corresponding to the fragments (D1, D2, and D3) of DFF45 generated by cleavage at the caspase consensus sites in DFF45. Either D1 or D2, as an isolated domain, is capable of inhibiting DFF40 nuclease activity while double domain fragments D1-2 and D2-3, as well as full-length DFF45, bind to DFF40 with high affinity and are much more effective inhibitors. The chaperone activity of DFF45 resides in part in its ability to maintain DFF40 as a soluble protein. In addition, D1 of DFF45 was found to be critical for the expression of active DFF40 in vivo, suggesting a role for DFF45 in binding nascent DFF40.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
McCarty JS,Toh SY,Li Pdoi
10.1006/bbrc.1999.1497subject
Has Abstractpub_date
1999-10-14 00:00:00pages
176-80issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(99)91497-3journal_volume
264pub_type
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