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J. Biol. Chem., Vol. 275, Issue 28, 21302-21308, July 14, 2000
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From the Apoptosis is characterized by various cell
morphological and biochemical features, one of which is the
internucleosomal degradation of genomic DNA. The role of the human
chromatin-bound Ca2+- and
Mg2+-dependent endonuclease (CME) DNAS1L3 and
its inhibition by poly(ADP-ribosyl)ation in the DNA degradation that
accompanies apoptosis was investigated. The nuclear localization of
this endonuclease is the unique feature that distinguishes it from
other suggested apoptotic nucleases. Purified recombinant DNAS1L3 was
shown to cleave nuclear DNA into both high molecular weight and
oligonucleosomal fragments in vitro. Furthermore, exposure
of mouse skin fibroblasts expressing DNAS1L3 to inducers of apoptosis
resulted in oligonucleosomal DNA fragmentation, an effect not observed
in cells not expressing this CME, as well as in a decrease in cell
viability greater than that apparent in the control cells. Recombinant
DNAS1L3 was modified by recombinant human poly(ADP-ribose) polymerase
(PARP) in vitro, resulting in a loss of nuclease activity.
The DNAS1L3 protein also underwent poly(ADP-ribosyl)ation in
transfected mouse skin fibroblasts in response to inducers of
apoptosis. The cleavage and inactivation of PARP by a caspase-3-like
enzyme late in apoptosis were associated with a decrease in the extent
of DNAS1L3 poly(ADP-ribosyl)ation, which likely releases DNAS1L3 from
inhibition and allows it to catalyze the degradation of genomic DNA.
A Role of the
Ca2+/Mg2+-dependent Endonuclease in
Apoptosis and Its Inhibition by Poly(ADP-ribose) Polymerase*
,,,,,¶
Department of Biochemistry and Molecular
Biology, Georgetown University School of Medicine, Washington, D. C. 20007 and the § Department of Biochemistry, Nara Medical
University, Kashihara, Japan
*
This work was supported by National Cancer Institute Grants
CA25344 and 1P01-CA74175, U.S. Air Force Office of Scientific Research
Grant AFOSR-89-0053, and U.S. Army Medical Research and Development
Command Contract DAMD17-90C-0053 (all to M. E. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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