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J Biol Chem, Vol. 275, Issue 11, 8091-8096, March 17, 2000
From the Caspase-activated DNase (CAD) is the enzyme that
causes DNA fragmentation during apoptosis. CAD forms aggregates when it
is synthesized in the absence of an inhibitor of CAD (ICAD). Here, using renaturation systems of chemically denatured CAD, we report that
ICAD-L, a long form of ICAD, has a chaperone-like activity specific for
CAD. Murine CAD carries 14 cysteines, most of which were found to be in
reduced form. Reducing agents enhanced the production of the functional
CAD in an in vitro translation system. The denatured
CAD could be efficiently renatured under highly reducing
conditions only in the presence of ICAD-L. This process was
ATP-independent. In contrast, reticulocyte lysates stimulated ICAD-L- and ATP-dependent renaturation of denatured CAD
without requiring a high concentration of reducing agents. These
results indicate that ICAD-L works not only as a specific inhibitor but also as a specific chaperone for CAD.
Specific Chaperone-like Activity of Inhibitor of
Caspase-activated DNase for Caspase-activated DNase*
§¶,
, and§**
Department of Genetics, Osaka University
Medical School and § Core Research for Evolutional
Science and Technology, Japan Science and Technology Corporation,
2-2 Yamada-oka, Suita, Osaka 565-0871, and Central
Laboratories for Key Technology, Kirin Brewery Company, Limited, 1-13-5 Fukuura, Kanazawa, Yokohama, Kanagawa 236-0004, Japan
*
This work was supported in part by Grants-in-aid from the
Ministry of Education, Science, Sports, and Culture in Japan.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.
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