Literature DB >> 1247505

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

E A Lewis, M S DeBuysere, A W Rees.   

Abstract

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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Year:  1976        PMID: 1247505     DOI: 10.1021/bi00646a029

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  11 in total

1.  Viscosity of chromatin solutions increases with increasing ionic strength.

Authors:  R Brust
Journal:  Mol Biol Rep       Date:  1986       Impact factor: 2.316

2.  Differences in the circular dichroism spectra of of eu- and heterochromatin fractions from rat liver.

Authors:  G H Moyer; E Kay; G E Austin
Journal:  Nucleic Acids Res       Date:  1979-04       Impact factor: 16.971

3.  Studies on the structure of isolated chromatin in three different solvents.

Authors:  H Hollandt; H Notbohm; F Riedel; E Harbers
Journal:  Nucleic Acids Res       Date:  1979       Impact factor: 16.971

4.  Circular dichroism analysis of mononucleosome DNA conformation.

Authors:  M K Cowman; G D Fasman
Journal:  Proc Natl Acad Sci U S A       Date:  1978-10       Impact factor: 11.205

5.  Viscosity as an additional physico-chemical parameter for studying chromatin structure.

Authors:  R Brust
Journal:  Mol Biol Rep       Date:  1985-10       Impact factor: 2.316

6.  Physicochemical properties of salt-soluble, unsheared chromatin. Molecular weight studies.

Authors:  M Böttger; H Fenske; L Karawajew; H Hamann; K Karawajew; R Lindigkeit
Journal:  Mol Biol Rep       Date:  1982-04-16       Impact factor: 2.316

7.  Structural transition in chromatin induced by ions in solution.

Authors:  H J Li; A W Hu; R A Maciewicz; P Cohen; R M Santella; C Chang
Journal:  Nucleic Acids Res       Date:  1977-11       Impact factor: 16.971

8.  Physicochemical properties of salt-soluble, unsheared chromatin. Salt-dependent structural changes.

Authors:  M Böttger; L Karawajew; H Fenske; K Grade; R Lindigkeit
Journal:  Mol Biol Rep       Date:  1981-08-14       Impact factor: 2.316

9.  Physical properties of nucleoprotein cores from adenovirus type 5.

Authors:  J A Harpst; J F Ennever; W C Russell
Journal:  Nucleic Acids Res       Date:  1977-02       Impact factor: 16.971

10.  Correlation between endogenous nucleosomal hyper(ADP-ribosyl)ation of histone H1 and the induction of chromatin relaxation.

Authors:  R J Aubin; A Fréchette; G de Murcia; P Mandel; A Lord; G Grondin; G G Poirier
Journal:  EMBO J       Date:  1983       Impact factor: 11.598

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