Clue to damage recognition by UvrB: residues in the beta-hairpin structure prevent binding to non-damaged DNA.

@article{Moolenaar2001ClueTD,
  title={Clue to damage recognition by UvrB: residues in the beta-hairpin structure prevent binding to non-damaged DNA.},
  author={Geri F. Moolenaar and Lotta H{\"o}glund and N. Goosen},
  journal={The EMBO journal},
  year={2001},
  volume={20 21},
  pages={
          6140-9
        }
}
UvrB, the ultimate damage-recognizing component of bacterial nucleotide excision repair, contains a flexible beta-hairpin rich in hydrophobic residues. We describe the properties of UvrB mutants in which these residues have been mutated. The results show that Y101 and F108 in the tip of the hairpin are important for the strand-separating activity of UvrB, supporting the model that the beta-hairpin inserts between the two DNA strands during the search for DNA damage. Residues Y95 and Y96 at the… CONTINUE READING

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 20 CITATIONS

Similar Papers

Loading similar papers…