Cooperative interaction of the C-terminal domain of histone H1 with DNA

Ana T. Rodríguez, Luís Pérez, Federico Morán, Francisco Montero, Pedro Suau

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15 Citations (Scopus)


We have studied the interaction of the isolated C-terminal domain of histone H1 with linear DNA using precipitation curves and electron microscopy. The C-terminal domain shows a salt-dependent transition towards cooperative binding, which reaches completion at 60 mM NaCI. At this salt concentration, the C-terminal domain binds to some of the DNA molecules, leaving the rest free. A binding site of 22 base-pairs can be calculated from the stoichiometry of the precipitated fractions. The C-terminal domain condenses the DNA in toroidal particles. The average inner radius of the particles is of the order of 195 Å. Consideration of the value of the inner radius of the toroids in the light of counterion condensation theory suggests that in these complexes the isolated C-terminal domain is capable of nearly full electrostatic neutralization of the DNA phosphate charge. © 1991.
Original languageEnglish
Pages (from-to)145-152
JournalBiophys. Chem.
Issue number2
Publication statusPublished - 1 Jan 1991


  • Binding cooperativity
  • C-terminal domain
  • DNA binding
  • DNA charge neutralization
  • Histone H1


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