Distinct DNA elements contribute to Rap1p affinity for its binding sites.

@article{Vescovo2004DistinctDE,
  title={Distinct DNA elements contribute to Rap1p affinity for its binding sites.},
  author={Valerio Del Vescovo and Veronica De Sanctis and Alessandro Bianchi and David Shore and Ernesto Di Mauro and Rodolfo Negri},
  journal={Journal of molecular biology},
  year={2004},
  volume={338 5},
  pages={877-93}
}
The essential Saccharomyces cerevisiae regulatory protein Rap1 contains two tandem Myb-like DNA binding sub-domains that interact with two defined DNA "hemisites", separated by a trinucleotide linker sequence. We have mapped the thermodynamically defined DNA-binding site of Rap1 by a primer extension method coupled with electrophoretic separation of bound and unbound DNAs. Relative to published consensus sequences, we detect binding interactions that extend 3 bp beyond the 5'-end of the… CONTINUE READING

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