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J. Biol. Chem., Vol. 276, Issue 44, 40652-40658, November 2, 2001
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From the Department of Pharmacology, University of Medicine and
Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway,
New Jersey 08854-5635 and the DNA topoisomerase II (TOP2) cleavable complexes
represent an unusual type of DNA damage characterized by reversible
TOP2-DNA cross-links and DNA double strand breaks. Many
antitumor drugs and physiological stresses are known to induce TOP2
cleavable complexes leading to apoptotic cell death and genomic
instability. However, the molecular mechanism(s) for repair of TOP2
cleavable complexes remains unclear. In the current studies, we show
that TOP2 cleavable complexes induced by the prototypic TOP2 poison VM-26 are proteolytically degraded by the ubiquitin/26 S proteasome pathway. Surprisingly the TOP2
26 S Proteasome-mediated Degradation of Topoisomerase II
Cleavable Complexes*
,, and Institute of Molecular
Biology, Academia Sinica, Taipei, Taiwan
isozyme is preferentially degraded over TOP2
isozyme. In addition, transcription inhibitors such as
5,6-dichlorobenzimidazole riboside and camptothecin can
substantially block VM-26-induced TOP2 degradation. These results
are consistent with a model in which the repair of TOP2 cleavable
complexes may involve transcription-dependent proteolysis
of TOP2 to reveal the protein-concealed double strand breaks.
*
This work was supported by National Institutes of Health
Grants GM27731 and CA 39662, Grant NSC 89-2320-B001-075 from the National Science Council of Taiwan, and Academia Sinica.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 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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