Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface.

@article{Marintcheva2008AcidicCT,
  title={Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface.},
  author={Boriana Marintcheva and Assen Marintchev and Gerhard Wagner and Charles C. Richardson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 6},
  pages={1855-60}
}
ssDNA-binding proteins are key components of the machinery that mediates replication, recombination, and repair. Prokaryotic ssDNA-binding proteins share a conserved DNA-binding fold and an acidic C-terminal tail. It has been proposed that in the absence of ssDNA, the C-terminal tail contacts the ssDNA-binding cleft, therefore predicting that the binding of ssDNA and the C-terminal tail is mutually exclusive. Using chemical cross-linking, competition studies, and NMR chemical-shift mapping, we… CONTINUE READING