A role for the base excision repair enzyme NEIL3 in replication-dependent repair of interstrand DNA cross-links derived from psoralen and abasic sites |
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| Institution: | 1. Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Department of Microbiology, Weigla 12, 53-114 Wroc?aw, Poland;2. Max Planck Institute for Molecular Genetics, Ihnestrasse 63-73, 14195 Berlin, Germany;3. University of Wroc?aw, Faculty of Biotechnology, Joliot-Curie 14a, 50-138 Wroc?aw, Poland;1. Comprehensive Cancer Center, Taichung Veterans General Hospital, Taichung, Taiwan;2. Department of Nursing, Taichung Veterans General Hospital, Taichung, Taiwan;3. Division of Thoracic Surgery, Department of Surgery, Taichung Veterans General Hospital, Taichung, Taiwan;4. Management Office for Health Data, China Medical University Hospital, Taichung, Taiwan;5. Graduate Institute of Clinical Medical Science, School of Medicine, College of Medicine, China Medical University, Taichung, Taiwan;6. School of Medicine, National Yang Ming University, Taipei, Taiwan;7. Department of Nuclear Medicine, PET Center, China Medical University Hospital, Taichung, Taiwan |
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| Abstract: | Interstrand DNA–DNA cross-links are highly toxic lesions that are important in medicinal chemistry, toxicology, and endogenous biology. In current models of replication-dependent repair, stalling of a replication fork activates the Fanconi anemia pathway and cross-links are “unhooked” by the action of structure-specific endonucleases such as XPF-ERCC1 that make incisions flanking the cross-link. This process generates a double-strand break, which must be subsequently repaired by homologous recombination. Recent work provided evidence for a new, incision-independent unhooking mechanism involving intrusion of a base excision repair (BER) enzyme, NEIL3, into the world of cross-link repair. The evidence suggests that the glycosylase action of NEIL3 unhooks interstrand cross-links derived from an abasic site or the psoralen derivative trioxsalen. If the incision-independent NEIL3 pathway is blocked, repair reverts to the incision-dependent route. In light of the new model invoking participation of NEIL3 in cross-link repair, we consider the possibility that various BER glycosylases or other DNA-processing enzymes might participate in the unhooking of chemically diverse interstrand DNA cross-links. |
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| Keywords: | DNA cross-link Cross-link repair Fanconi anemia Homologous recombination Base excision repair XPF-ERCC1 NEIL Abasic site Psoralen |
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