Identification of an amino acid–base contact in the GCN4–DNA complex by bromouracil-mediated photocrosslinking

@article{Blatter1992IdentificationOA,
  title={Identification of an amino acid–base contact in the GCN4–DNA complex by bromouracil-mediated photocrosslinking},
  author={E. Blatter and Y. Ebright and R. Ebright},
  journal={Nature},
  year={1992},
  volume={359},
  pages={650-652}
}
THE bZIP DNA-binding proteins are characterized by a 50-amino-acid DNA binding and dimerization motif, consisting of a highly basic DNA-binding region ('b') followed by a leucine zipper dimerization region ('ZIP')1. The best characterized bZIP DNA-binding protein is GCN4, a yeast transcriptional activator2–6. GCN4 binds to a 9-base-pair two-fold-symmetric DNA site, 5'−A−4T−3G−2A−1C0T+1C+2A+3T+4−3' (refs 7–10). A detailed model known as the 'induced helical fork' model has been proposed for the… Expand
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Photoaffinity labelling of a DNA-binding site on the globular domain of histone H5.
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References

SHOWING 1-10 OF 29 REFERENCES
Molecular characterization of the GCN4-DNA complex.
...
1
2
3
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