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Papers In Press, published online ahead of print August 23, 2001
Department of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854
Corresponding Author: lliu{at}umdnj.edu
DNA topoisomerase II (TOP2) cleavable complexes represent an unusual type of DNA damage characterized by reversible TOP2-DNA crosslinks 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/26S proteasome pathway. Surprisingly, the TOP2beta isozyme is preferentially degraded over TOP2alpha isozyme. In addition, transcription inhibitors such as DRB and camptothecin can substantially block VM-26-induced TOP2beta degradation. These results are consistent with a model in which repair of TOP2beta cleavable complexes may involve transcription-dependent proteolysis of TOP2beta to reveal the protein-concealed double-strand breaks.
J. Biol. Chem, 10.1074/jbc.M104009200
Submitted on May 3, 2001
Revised on August 23, 2001
Accepted on August 22, 2001
26S proteasome-mediated degradation of topoisomerase II cleavable complexes
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