Allostery and Intrinsic Disorder Mediate Transcription Regulation by Conditional Cooperativity

@article{GarciaPino2010AllosteryAI,
  title={Allostery and Intrinsic Disorder Mediate Transcription Regulation by Conditional Cooperativity},
  author={Abel Garcia-Pino and Sreeram Balasubramanian and Lode Wyns and Ehud Gazit and Henri De Greve and Roy David Magnuson and Daniel Charlier and Nico A. J. van Nuland and Remy Loris},
  journal={Cell},
  year={2010},
  volume={142},
  pages={101-111}
}
Regulation of the phd/doc toxin-antitoxin operon involves the toxin Doc as co- or derepressor depending on the ratio between Phd and Doc, a phenomenon known as conditional cooperativity. The mechanism underlying this observed behavior is not understood. Here we show that monomeric Doc engages two Phd dimers on two unrelated binding sites. The binding of Doc to the intrinsically disordered C-terminal domain of Phd structures its N-terminal DNA-binding domain, illustrating allosteric coupling… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 74 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 40 references

Interactions between the toxin Kid of the bacterial parD system and the antitoxins Kis and MazE

  • M. B. Kamphuis, M. C. Monti, +6 authors R. Boelens
  • Proteins
  • 2007
1 Excerpt

Similar Papers

Loading similar papers…