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Papers In Press, published online ahead of print November 27, 2001
Department of Genetics, Osaka University Medical School, Suita, Osaka 565-0871
Corresponding Author: nagata{at}genetic.med.osaka-u.ac.jp
CAD (caspase-activated DNase) that causes chromosomal DNA fragmentation during apoptosis exists as a complex with ICAD (inhibitor of CAD) in proliferating cells. Here, we report that denatured CAD is functionally refolded with Hsc70-Hsp40 and ICAD. Hsc70-Hsp40 suppresses the aggregation of the denatured CAD, but can not restore its enzymatic activity. In contrast, ICAD could not suppress the aggregation of CAD, but supported the CAD?s renaturation with Hsc70-Hsp40, indicating that ICAD recognizes the quasi-native folding state of CAD that is conferred by Hsc70-Hsp40. Using an in vitro translation system, we then showed that during CAD translation, Hsc70-Hsp40 as well as ICAD bind to the nascent CAD polypeptide, while on ribosomes. These results indicate that ICAD together with Hsc70-Hsp40 assists the folding of CAD during its synthesis, and that the CAD/ICAD heterodimer is formed co-translationally.
J. Biol. Chem, 10.1074/jbc.M110071200
Submitted on October 18, 2001
Revised on November 19, 2001
Accepted on November 27, 2001
Co-translational folding of caspase-activated DNase with Hsp70, Hsp40 and inhibitor of caspase-activated DNase
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