Recognition of DNA damage by XPC coincides with disruption of the XPC–RAD23 complex
Copyright policy )Recognition of DNA damage by XPC coincides with disruption of the XPC–RAD23 complex
The recognition of helix-distorting deoxyribonucleic acid (DNA) lesions by the global genome nucleotide excision repair subpathway is performed by the XPC–RAD23–CEN2 complex. Although it has been established that Rad23 homologs are essential to protect XPC from proteasomal degradation, it is unclear whether RAD23 proteins have a direct role in the recognition of DNA damage. In this paper, we show that the association of XPC with ultraviolet-induced lesions was impaired in the absence of RAD23 proteins. Furthermore, we show that RAD23 proteins rapidly dissociated from XPC upon binding to damaged DNA. Our data suggest that RAD23 proteins facilitate lesion recognition by XPC but do not participate in the downstream DNA repair process.
- Karolinska Institute Sweden
- Erasmus University Medical Center Netherlands
- University of Groningen Netherlands
- Erasmus University Rotterdam Netherlands
GROUP-C PROTEIN, RECRUITMENT, Cell Nucleus, STABILITY, DNA Repair, XERODERMA-PIGMENTOSUM, HUMAN-CELLS, DNA, EMC MM-03-24-01, MECHANISMS, Cell Line, ACTIVATION, DNA-Binding Proteins, Mice, NUCLEOTIDE EXCISION-REPAIR, BINDING, Animals, Humans, EMC MGC-01-12-03, RAD23, Research Articles, DNA Damage
GROUP-C PROTEIN, RECRUITMENT, Cell Nucleus, STABILITY, DNA Repair, XERODERMA-PIGMENTOSUM, HUMAN-CELLS, DNA, EMC MM-03-24-01, MECHANISMS, Cell Line, ACTIVATION, DNA-Binding Proteins, Mice, NUCLEOTIDE EXCISION-REPAIR, BINDING, Animals, Humans, EMC MGC-01-12-03, RAD23, Research Articles, DNA Damage
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