Cooperative interaction of the C-terminal domain of histone H1 with DNA.
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 NaCl. 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 A. 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.
Rodríguez
A T
AT
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Autónoma de Barcelona, Spain.
Pérez
L
L
Morán
F
F
Montero
F
F
Suau
P
P
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002627:Chemistry, Physical; D004247:DNA / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D006657:Histones / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D011487:Protein Conformation
D006657:Histones; D004247:DNA