The role of ATP binding and hydrolysis by UvrB during nucleotide excision repair.

@article{Moolenaar2000TheRO,
  title={The role of ATP binding and hydrolysis by UvrB during nucleotide excision repair.},
  author={Geri F. Moolenaar and Michael M. Herron and Vincenzo Monaco and Gijs A. van der Marel and Jacques H. van Boom and Robert Visse and N. Goosen},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 11},
  pages={
          8044-50
        }
}
We have isolated UvrB-DNA complexes by capture of biotinylated damaged DNA substrates on streptavidin-coated magnetic beads. With this method the UvrB-DNA preincision complex remains stable even in the absence of ATP. For the binding of UvrC to the UvrB-DNA complex no cofactor is needed. The subsequent induction of 3' incision does require ATP binding by UvrB but not hydrolysis. This ATP binding induces a conformational change in the DNA, resulting in the appearance of the DNase I… CONTINUE READING
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