期刊
MOLECULAR CELL
卷 64, 期 2, 页码 376-387出版社
CELL PRESS
DOI: 10.1016/j.molcel.2016.09.005
关键词
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资金
- NIH [5R01ES019566, 5R01ES024872, 5R01ES002614, 2P30CA047904]
- National Science Foundation [MCB-1412692]
- Biotechnology and Biological Sciences Research Council [BB/I003460/1] Funding Source: researchfish
- BBSRC [BB/I003460/1] Funding Source: UKRI
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 the 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 or constrained motion. Atomic force microcopy analysis of Rad4 with the beta-hairpin domain 3 (BHD3) deleted reveals that this motif is non-essential for damage-specific binding and DNA bending. Furthermore, we find that deletion of seven residues in the tip of b-hairpin in BHD3 increases Rad4-Rad23 constrained motion at the expense of stable binding at sites of DNA lesions, without diminishing cellular UV resistance or photoproduct repair in vivo. These results suggest a distinct intermediate in the damage recognition process during NER, allowing dynamic DNA damage detection at a distance.
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