Action of apoptotic endonuclease DNase gamma on naked DNA and chromatin substrates.

Abstract:

:The internucleosomal cleavage of genomic DNA is a biochemical hallmark of apoptosis. DNase gamma, 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 gamma, we showed that DNase gamma 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 gamma is restricted, but its activity is enhanced in the presence of linker histone H1, which explains DNA cleavage at linker regions of apoptotic nuclei.

authors

Mizuta R,Mizuta M,Araki S,Shiokawa D,Tanuma S,Kitamura D

doi

10.1016/j.bbrc.2006.04.107

subject

Has Abstract

pub_date

2006-06-30 00:00:00

pages

560-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00907-7

journal_volume

345

pub_type

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