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. 1981 Mar 11;9(5):1053–1068. doi: 10.1093/nar/9.5.1053

Stability of the primary organization of nucleosome core particles upon some conformational transitions.

V W Zayetz, S G Bavykin, V L Karpov, A D Mirzabekov
PMCID: PMC326736  PMID: 7232210

Abstract

The sequential arrangement of histones along DNA in nucleosome core particles was determined between 0.5 and 600 mM salt and from 0 to 8 M urea. These concentrations of salt and urea up to 6 M had no significant effect on the linear order of histones along DNA but 8 M urea caused the rearrangement of histones. Conformational changes in cores have been identified within these ranges of conditions by several laboratories 8-21. Also, abrupt structural changes in the cores, apparently their unfolding, were found by gel electrophoresis to occur at urea concentration, between 4 and 5 M. 600 mM salt and 6 M urea were shown to relax the binding of histones to DNA in cores but do not however release histones or some part of their molecules from DNA. It appears therefore that nucleosomal cores can undergo some conformational transitions and unfolding whereas their primary organization remains essentially unaffected. These results are consistent with a model of the core particles in which the histone octamer forms something like a helical "rim" along the superhelical DNA and histone-histone interactions beyond the "rim" are rather weak in comparison with those within the "rim".

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Selected References

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

  1. Bolund L. A., Johns E. W. The selective extraction of histone fractions from deoxyribonucleoprotein. Eur J Biochem. 1973 Jun 15;35(3):546–553. doi: 10.1111/j.1432-1033.1973.tb02871.x. [DOI] [PubMed] [Google Scholar]
  2. Cary P. D., Moss T., Bradbury E. M. High-resolution proton-magnetic-resonance studies of chromatin core particles. Eur J Biochem. 1978 Sep 1;89(2):475–482. doi: 10.1111/j.1432-1033.1978.tb12551.x. [DOI] [PubMed] [Google Scholar]
  3. Creighton T. E. Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J Mol Biol. 1980 Feb 15;137(1):61–80. doi: 10.1016/0022-2836(80)90157-6. [DOI] [PubMed] [Google Scholar]
  4. Dieterich A. E., Axel R., Cantor C. R. Salt-induced structural changes of nucleosome core particles. J Mol Biol. 1979 Apr 25;129(4):587–602. doi: 10.1016/0022-2836(79)90470-4. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Elgin S. C., Hood L. E. Chromosomal proteins of Drosophila embryos. Biochemistry. 1973 Nov 20;12(24):4984–4991. doi: 10.1021/bi00748a026. [DOI] [PubMed] [Google Scholar]
  7. Finch J. T., Lutter L. C., Rhodes D., Brown R. S., Rushton B., Levitt M., Klug A. Structure of nucleosome core particles of chromatin. Nature. 1977 Sep 1;269(5623):29–36. doi: 10.1038/269029a0. [DOI] [PubMed] [Google Scholar]
  8. Glover J. S., Salter D. N., Shepherd B. P. A study of some factors that influence the iodination of ox insulin. Biochem J. 1967 Apr;103(1):120–128. doi: 10.1042/bj1030120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Hardison R. C., Zeitler D. P., Murphy J. M., Chalkley R. Histone neighbors in nuclei and extended chromatin. Cell. 1977 Oct;12(2):417–427. doi: 10.1016/0092-8674(77)90118-0. [DOI] [PubMed] [Google Scholar]
  11. Klug A., Rhodes D., Smith J., Finch J. T., Thomas J. O. A low resolution structure for the histone core of the nucleosome. Nature. 1980 Oct 9;287(5782):509–516. doi: 10.1038/287509a0. [DOI] [PubMed] [Google Scholar]
  12. Lohr D., Van Holde K. E. Organization of spacer DNA in chromatin. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6326–6330. doi: 10.1073/pnas.76.12.6326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Martinson H. G., True R. J. On the mechanism of nucleosome unfolding. Biochemistry. 1979 Mar 20;18(6):1089–1094. doi: 10.1021/bi00573a024. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Olins D. E., Bryan P. N., Harrington R. E., Hill W. E., Olins A. L. Conformational states of chromatin nu bodies induced by urea. Nucleic Acids Res. 1977 Jun;4(6):1911–1931. doi: 10.1093/nar/4.6.1911. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pardon J. F., Worcester D. L., Wooley J. C., Cotter R. I., Lilley D. M., Richards R. M. The structure of the chromatin core particle in solution. Nucleic Acids Res. 1977 Sep;4(9):3199–3214. doi: 10.1093/nar/4.9.3199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Prunell A., Kornberg R. D., Lutter L., Klug A., Levitt M., Crick F. H. Periodicity of deoxyribonuclease I digestion of chromatin. Science. 1979 May 25;204(4395):855–858. doi: 10.1126/science.441739. [DOI] [PubMed] [Google Scholar]
  19. Shick V. V., Belyavsky A. V., Bavykin S. G., Mirzabekov A. D. Primary organization of the nucleosome core particles. Sequential arrangement of histones along DNA. J Mol Biol. 1980 May 25;139(3):491–517. doi: 10.1016/0022-2836(80)90143-6. [DOI] [PubMed] [Google Scholar]
  20. Shindo H., McGhee J. D., Cohen J. S. 31P-NMR studies of DNA in nucleosome core particles. Biopolymers. 1980 Mar;19(3):523–537. doi: 10.1002/bip.1980.360190307. [DOI] [PubMed] [Google Scholar]
  21. Suau P., Kneale G. G., Braddock G. W., Baldwin J. P., Bradbury E. M. A low resolution model for the chromatin core particle by neutron scattering. Nucleic Acids Res. 1977 Nov;4(11):3769–3786. doi: 10.1093/nar/4.11.3769. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Thoma F., Koller T., Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol. 1979 Nov;83(2 Pt 1):403–427. doi: 10.1083/jcb.83.2.403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Trifonov E. The helical model of the nucleosome core. Nucleic Acids Res. 1978 Apr;5(4):1371–1380. doi: 10.1093/nar/5.4.1371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Varshavsky A. J., Bakayev V. V., Georgiev G. P. Heterogeneity of chromatin subunits in vitro and location of histone H1. Nucleic Acids Res. 1976 Feb;3(2):477–492. doi: 10.1093/nar/3.2.477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weintraub H., Worcel A., Alberts B. A model for chromatin based upon two symmetrically paired half-nucleosomes. Cell. 1976 Nov;9(3):409–417. doi: 10.1016/0092-8674(76)90085-4. [DOI] [PubMed] [Google Scholar]
  26. Wong N. T., Candido E. P. Histone H3 thiol reactivity as a probe of nucleosome structure. J Biol Chem. 1978 Nov 25;253(22):8263–8268. [PubMed] [Google Scholar]
  27. Woodcock C. L., Frado L. L. Ultrastructure of chromatin subunits during unfolding, histone depletion, and reconstitution. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 1):43–55. doi: 10.1101/sqb.1978.042.01.007. [DOI] [PubMed] [Google Scholar]
  28. 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]
  29. Yaneva M., Dessev G. Persistence of the ten-nucleotide repeat in chromatin unfolded in urea, as revealed by digestion with deoxyribonuclease i. Nucleic Acids Res. 1976 Jul;3(7):1761–1767. doi: 10.1093/nar/3.7.1761. [DOI] [PMC free article] [PubMed] [Google Scholar]

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