On the heterogeneity of chromatin fractions after gel filtration

Labourdette, G.; Raynaud, André; Roizes, Gérard; Ohlenbusch, Heiko H.

doi:10.1016/0022-2836(74)90519-1

Cited by 2 publications

(1 citation statement)

References 26 publications

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“…However, it is also clear that the protein/DNA ratio of the leading peak varies across the peak, implying an incipient tendency for a new equilibrium to be established across this peak as it moves down the column. This phenomenon has been noted previously by us [7] and by others [15]. Despite this, an accurate measure of the amount of protein bound to the DNA in the original equilibrium may be obtained by pooling all the fractions from the first peak and measuring the overall protein-DNA ratio.In this way the curve for histone dissociation between 1.0 and 2.0 M NaC1 at 4°C was constructed ( fig.2).…”

Section: Resultssupporting

confidence: 51%

Histones F2a1 and F3 interact reversibly and cooperatively with DNA to form an equimolar complex in chromatin

1975

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Section: Resultssupporting

confidence: 51%

Histones F2a1 and F3 interact reversibly and cooperatively with DNA to form an equimolar complex in chromatin

1975

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Configuration of unsheared nucleohistone. Effects of ionic strength and of histone F1 removal

Lewis¹,

DeBuysere²,

Rees³

1976

Biochemistry

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Nucleohistone solubilized from rabbit thymus nuclei by an endogenous nuclease has in 0.15 M salt an exceptionally low intrinsic viscosity and very high sedimentation velocity. A fully reversible expansion of configuration occurs on lowering ionic strength. When [eta] is plotted against I-1/2 and extrapolated to high I, [eta] = 0 is reached at I = 0.4-1 M and [eta] at I = infinity is negative, contrary to the behavior of DNA and of the great majority of polyelectrolytes, which extrapolate to a positive [eta] at I = infinity. This behavior demands that the configuration of nucleohistone depends not only on electrostatic expansive forces but also on contracting forces which are not electrostatic and do not go to zero in any accessible configuration. Intramolecular hydrophobic bonds might provide such contracting forces. Increasing I above 0.15 M leads to precipitation near 0.3 M and redissolution with dissociation of F1 and expansion in 0.6 M. The expansion is largely but not completely reversed on return to 0.15 M. Much further expansion occurs in I = 1.2 M. Nucleohistone exposed to 1.2 M could not be redissolved in the original medium. Nucleohistone depleted of F1 exhibits a similar expansion as ionic strength is reduced, at higher viscosities throughout. On extrapolation to I = infinity both positive and negative viscosities were observed, on different lots, perhaps reflecting variable extraction of other histones. Circular dichroism spectra are very little affected by ionic strength (0.6 M and lower) or F1 removal, despite tenfold changes in viscosity.

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On the heterogeneity of chromatin fractions after gel filtration

Cited by 2 publications

References 26 publications

Histones F2a1 and F3 interact reversibly and cooperatively with DNA to form an equimolar complex in chromatin

Histones F2a1 and F3 interact reversibly and cooperatively with DNA to form an equimolar complex in chromatin

Configuration of unsheared nucleohistone. Effects of ionic strength and of histone F1 removal

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