Recruitment of the transcriptional machinery through GAL11P: structure and interactions of the GAL4 dimerization domain.

@article{Hidalgo2001RecruitmentOT,
  title={Recruitment of the transcriptional machinery through GAL11P: structure and interactions of the GAL4 dimerization domain.},
  author={Paulina Hidalgo and Aseem Z Ansari and P. R. L. Schmidt and Brian Hare and Natasha Simkovich and Susan Farrell and Eun Ji Shin and Mark Ptashne and Gerhard Wagner},
  journal={Genes & development},
  year={2001},
  volume={15 8},
  pages={1007-20}
}
The GAL4 dimerization domain (GAL4-dd) is a powerful transcriptional activator when tethered to DNA in a cell bearing a mutant of the GAL11 protein, named GAL11P. GAL11P (like GAL11) is a component of the RNA-polymerase II holoenzyme. Nuclear magnetic resonance (NMR) studies of GAL4-dd revealed an elongated dimer structure with C(2) symmetry containing three helices that mediate dimerization via coiled-coil contacts. The two loops between the three coiled coils form mobile bulges causing a… CONTINUE READING

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