Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1987 Aug 25;15(16):6655–6664. doi: 10.1093/nar/15.16.6655

Reversibility of the low-salt transition of chromatin core particles.

L J Libertini, E W Small
PMCID: PMC306129  PMID: 3628003

Abstract

The low-salt transition of chromatin core particles is reversible if the monovalent cation concentration is kept above 0.2 mM. Exposure of the particles to salt concentrations below this value results in a nonreversible secondary transition. The nonreversible changes are relatively slow with a half-time of about 15 minutes. Once exposed to such low ionic strength, the particles then begin to refold with increasing salt in at least two steps over a much higher ionic strength range than is required for the usual low-salt transition. The refolding is very fast, with a half-time less than a minute. Small differences between particles which had or had not been exposed to very low salt persist even when the particles are returned to near physiological ionic strengths.

Full text

PDF
6655

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burch J. B., Martinson H. G. Iodination of nucleosomes at low ionic strength: conformational changes in H4 and stabilization by H1. Nucleic Acids Res. 1981 Sep 11;9(17):4367–4385. doi: 10.1093/nar/9.17.4367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dieterich A. E., Eshaghpour H., Crothers D. M., Cantor C. R. Effect of DNA length on the nucleosome low salt transition. Nucleic Acids Res. 1980 Jun 11;8(11):2475–2487. doi: 10.1093/nar/8.11.2475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Gordon V. C., Knobler C. M., Olins D. E., Schumaker V. N. Conformational changes of the chromatin subunit. Proc Natl Acad Sci U S A. 1978 Feb;75(2):660–663. doi: 10.1073/pnas.75.2.660. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Harrington R. E. Optical model studies of salt-induced conformational transitions in the nucleosome. Biochemistry. 1982 Mar 16;21(6):1177–1186. doi: 10.1021/bi00535a011. [DOI] [PubMed] [Google Scholar]
  5. Harrington R. E. Structural conformations of nucleosomes at low ionic strength from flow birefringence and intrinsic viscosity. Biopolymers. 1981 Apr;20(4):719–752. doi: 10.1002/bip.1981.360200408. [DOI] [PubMed] [Google Scholar]
  6. Libertini L. J., Small E. W. Effects of pH on low-salt transition of chromatin core particles. Biochemistry. 1982 Jul 6;21(14):3327–3334. doi: 10.1021/bi00257a013. [DOI] [PubMed] [Google Scholar]
  7. Martinson H. G., True R. J., Burch J. B. Specific histone-histone contacts are ruptured when nucleosomes unfold at low ionic strength. Biochemistry. 1979 Mar 20;18(6):1082–1089. doi: 10.1021/bi00573a023. [DOI] [PubMed] [Google Scholar]
  8. McGhee J. D., Felsenfeld G. Nucleosome structure. Annu Rev Biochem. 1980;49:1115–1156. doi: 10.1146/annurev.bi.49.070180.005343. [DOI] [PubMed] [Google Scholar]
  9. Schlessinger F. B., Dattagupta N., Crothers D. M. Unfolding of 175-base-pair nucleosomes. Biochemistry. 1982 Feb 16;21(4):664–669. doi: 10.1021/bi00533a012. [DOI] [PubMed] [Google Scholar]
  10. Simpson R. T. Modulation of nucleosome structure by histone subtypes in sea urchin embryos. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6803–6807. doi: 10.1073/pnas.78.11.6803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Wu H. M., Dattagupta N., Hogan M., Crothers D. M. Structural changes of nucleosomes in low-salt concentrations. Biochemistry. 1979 Sep 4;18(18):3960–3965. doi: 10.1021/bi00585a018. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES