Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding.

@article{Zhang2005Gly103IT,
  title={Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding.},
  author={Xiao-Ping Zhang and Kyung-Im Lee and Jachen A. Solinger and Konstantin Kiianitsa and Wolf-Dietrich Heyer},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 28},
  pages={26303-11}
}
Rad51 is a homolog of the bacterial RecA protein and is central for recombination in eukaryotes performing homology search and DNA strand exchange. Rad51 and RecA share a core ATPase domain that is structurally similar to the ATPase domains of helicases and the F1 ATPase. Rad51 has an additional N-terminal domain, whereas RecA protein has an additional C-terminal domain. Here we show that glycine 103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 is important for binding to single… CONTINUE READING

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DNA Repair and Mutagenesis, American Society for Microbiology

  • E. C. Friedberg, G. C. Walker, W. Siede
  • 1995

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