Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates.

@article{Witte2008StructuralBO,
  title={Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates.},
  author={Gregor Witte and Sophia Hartung and Katharina Buettner and Karl-Peter Hopfner},
  journal={Molecular cell},
  year={2008},
  volume={30 2},
  pages={
          167-78
        }
}
To reveal mechanisms of DNA damage checkpoint initiation, we structurally and biochemically analyzed DisA, a protein that controls a Bacillus subtilis sporulation checkpoint in response to DNA double-strand breaks. We find that DisA forms a large octamer that consists of an array of an uncharacterized type of nucleotide-binding domain along with two DNA-binding regions related to the Holliday junction recognition protein RuvA. Remarkably, the nucleotide-binding domains possess diadenylate… CONTINUE READING
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