A monomer-dimer equilibrium modulates the interaction of the sunflower homeodomain leucine-zipper protein Hahb-4 with DNA.

@article{Palena1999AME,
  title={A monomer-dimer equilibrium modulates the interaction of the sunflower homeodomain leucine-zipper protein Hahb-4 with DNA.},
  author={Claudia M. Palena and Daniel H{\'e}ctor Gonz{\'a}lez and Raquel L{\'i}a Chan},
  journal={The Biochemical journal},
  year={1999},
  volume={341 ( Pt 1)},
  pages={
          81-7
        }
}
We have analysed the interaction of the sunflower homeodomain leucine-zipper (Hd-Zip) protein Hahb-4 with DNA. The complete Hd-Zip domain from Hahb-4 was able to select specific sequences from a random oligonucleotide mixture that contained a 9-bp core with four fixed and five degenerate positions. Analysis of the binding of some of the selected sequences suggests that Hahb-4 preferentially binds the dyad-symmetrical sequence CAAT(A/T)ATTG. Single-nucleotide replacements at positions 1, 5 or 9… CONTINUE READING
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