The effect of histone H1 on the compaction of oligonucleosomes. A quasielastic light scattering study.
The structural properties of H1-depleted oligonucleosomes are investigated by the use of quasielastic laser light scattering, thermal denaturation and circular dichroism and compared to those of H1-containing oligomers. To obtain information on the role of histone H1 in compaction of nucleosomes, translational diffusion coefficients (D) are determined for mono-to octanucleosomes over a range of ionic strength. The linear dependences of D on the number of nucleosomes show that the conformation of stripped oligomers is very extended and does not change drastically with increasing the ionic strength while the rigidness of the chain decreases due to the folding of linker DNA. The results prove that the salt-induced condensation is much smaller for H1-depleted than for H1-containing oligomers and that histone H1 is necessary for the formation of a supercoiled structure of oligonucleosomes, already present at low ionic strength.
D000818:Animals; D002843:Chromatin / Q000378:metabolism; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006358:Hot Temperature; D066298:In Vitro Techniques; D008027:Light; D008099:Liver / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D051381:Rats; D012542:Scattering, Radiation
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA