Association of DFF40 with chromatin

Stable Identifier
Reaction [binding]
Homo sapiens
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Direct interactions between the histone H1 C-terminal domain and DFF40/CAD possibly target the nuclease to chromatin linker DNA promoting the linker DNA cleavage during the terminal stages of apoptosis (Widlak et al., 2005). Noteworthy, it has been reported that DFF40/DFF45 complexes could also associate with chromatin and be activated with caspase-3 in DNA-bound state (Korn et al., 2005).

Literature References
PubMed ID Title Journal Year
10318789 Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1

Liu, X, Zou, H, Widlak, P, Garrard, W, Wang, X

J Biol Chem 1999
15910001 The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage

Widlak, P, Kalinowska, M, Parseghian, MH, Lu, X, Hansen, JC, Garrard, WT

Biochemistry 2005
Participant Of
Orthologous Events
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