Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process.
作者： Muwen Kong , Lili Liu , Xuejing Chen , Katherine I Driscoll , Peng Mao
DOI: 10.1016/J.MOLCEL.2016.09.005
关键词:
摘要: Nucleotide excision repair (NER) is an evolutionarily conserved mechanism that processes helix-destabilizing and/or -distorting DNA lesions, such as UV-induced photoproducts. Here, we investigate the dynamic protein-DNA interactions during damage recognition step using single-molecule fluorescence microscopy. Quantum dot-labeled Rad4-Rad23 (yeast XPC-RAD23B ortholog) forms non-motile complexes or conducts a one-dimensional search via either random diffusion constrained motion. Atomic force microcopy analysis of Rad4 with β-hairpin domain 3 (BHD3) deleted reveals this motif non-essential for damage-specific binding and bending. Furthermore, we find deletion seven residues in tip BHD3 increases motion at expense stable sites without diminishing cellular UV resistance photoproduct in vivo. These results suggest distinct intermediate process NER, allowing detection distance.
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