Kinetic studies of the TATA-binding protein interaction with cisplatin-modified DNA.

@article{Jung2001KineticSO,
  title={Kinetic studies of the TATA-binding protein interaction with cisplatin-modified DNA.},
  author={Yongwon Jung and Yuji Mikata and Stephen J Lippard},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 47},
  pages={43589-96}
}
The TATA-binding protein (TBP) recognizes the TATA box element of transcriptional promoters and recruits other initiation factors. This essential protein binds selectively to cisplatin-damaged DNA. Electrophoretic mobility shift assays were performed to study the kinetics of TBP binding both to the TATA box and to cisplatin-damaged DNA in different sequence contexts. TBP binds with high affinity (K(d) = 0.3 nm) to DNA containing site-specific cisplatin 1,2-intrastrand d(GpG) cross-links. The k… CONTINUE READING

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