| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1940272 | Biochemical and Biophysical Research Communications | 2006 | 8 Pages |
Abstract
The internucleosomal cleavage of genomic DNA is a biochemical hallmark of apoptosis. DNase γ, a Mg2+/Ca2+-dependent endonuclease, has been suggested to be one of the apoptotic endonucleases, but its biochemical characteristic has not been fully elucidated. Here, using recombinant DNase γ, we showed that DNase γ is a Mg2+/Ca2+-dependent single-stranded DNA nickase and has a high activity at low ionic strength. Under higher ionic strength, such as physiological buffer conditions, the endonuclease activity of DNase γ is restricted, but its activity is enhanced in the presence of linker histone H1, which explains DNA cleavage at linker regions of apoptotic nuclei.
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Authors
Ryushin Mizuta, Midori Mizuta, Shinsuke Araki, Daisuke Shiokawa, Sei-ichi Tanuma, Daisuke Kitamura,