Journal
JOURNAL OF CELL BIOLOGY
Volume 197, Issue 2, Pages 267-281Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201106074
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Funding
- Swedish Cancer Society
- European Community Network of Excellence RUBICON [LSHC-CT-2005-018683]
- Swedish Research Council
- Netherlands Organization for Scientific Research [ZonMw 40-00812-98-08031]
- European Molecular Biology Organization (EMBO)
- Federation of European Biochemical Societies (FEBS)
- Human Frontier Science Program (HFSP)
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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.
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