| First Author | Luijsterburg MS | Year | 2012 |
| Journal | J Cell Biol | Volume | 197 |
| Issue | 2 | Pages | 267-81 |
| PubMed ID | 22492724 | Mgi Jnum | J:185041 |
| Mgi Id | MGI:5427276 | Doi | 10.1083/jcb.201106074 |
| Citation | Luijsterburg MS, et al. (2012) DDB2 promotes chromatin decondensation at UV-induced DNA damage. J Cell Biol 197(2):267-81 |
| abstractText | Nucleotide excision repair (NER) is the principal pathway that removes helix-distorting deoxyribonucleic acid (DNA) damage from the mammalian genome. Recognition of DNA lesions by xeroderma pigmentosum group C (XPC) protein in chromatin is stimulated by the damaged DNA-binding protein 2 (DDB2), which is part of a CUL4A-RING ubiquitin ligase (CRL4) complex. In this paper, we report a new function of DDB2 in modulating chromatin structure at DNA lesions. We show that DDB2 elicits unfolding of large-scale chromatin structure independently of the CRL4 ubiquitin ligase complex. Our data reveal a marked adenosine triphosphate (ATP)-dependent reduction in the density of core histones in chromatin containing UV-induced DNA lesions, which strictly required functional DDB2 and involved the activity of poly(adenosine diphosphate [ADP]-ribose) polymerase 1. Finally, we show that lesion recognition by XPC, but not DDB2, was strongly reduced in ATP-depleted cells and was regulated by the steady-state levels of poly(ADP-ribose) chains. |
