Condensation of DNA by the C-terminal domain of histone H1. A circular dichroism study.
The condensation of DNA by the C-terminal domain of histone H1 has been studied by circular dichroism in physiological salt concentration (0.14 M NaF). As the intact H1 molecule, its C-terminal domain induces the so-called psi state of DNA that is characterized by a nonconservative circular dichroism spectrum which is currently attributed to ordered aggregation of the DNA molecules. On a molar basis, intact H1 and its C-terminal domain give spectra of similar intensity. Neither the globular domain of H1 nor an N-terminal fragment, that includes both the globular and N-terminal domains, has any effect on the conservative circular dichroism of DNA. From these results it is concluded that the condensation of DNA mediated by histone H1 is mainly due to its C-terminal domain. The effect of the salt concentration and the size of DNA molecules on the circular dichroism of the complexes are also examined.
D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000378:metabolism; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D009690:Nucleic Acid Conformation; D009994:Osmolar Concentration; D010446:Peptide Fragments / Q000378:metabolism
D002843:Chromatin; D006657:Histones; D010446:Peptide Fragments; D004247:DNA