Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex
作者： Andrea Scrima , Renata Koníčková , Bryan K. Czyzewski , Yusuke Kawasaki , Philip D. Jeffrey
DOI: 10.1016/J.CELL.2008.10.045
关键词:
摘要: Ultraviolet (UV) light-induced pyrimidine photodimers are repaired by the nucleotide excision repair pathway. Photolesions have biophysical parameters closely resembling undamaged DNA, impeding discovery through damage surveillance proteins. The DDB1-DDB2 complex serves in initial detection of UV lesions vivo. Here we present structures alone and bound to DNA containing either a 6-4 pyrimidine-pyrimidone photodimer (6-4PP) lesion or an abasic site. structure shows that is held exclusively WD40 domain DDB2. A DDB2 hairpin inserts into minor groove, extrudes binding pocket, kinks duplex approximately 40 degrees. tightly localized probing photolesions, combined with proofreading enables detect refractory other provides insights recognition chromatin suggests mechanism which DDB1-associated CUL4 ubiquitin ligase targets proteins surrounding site damage.
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