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