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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1975 Jul;72(7):2626–2630. doi: 10.1073/pnas.72.7.2626

An octamer of histones in chromatin and free in solution.

J O Thomas, R D Kornberg
PMCID: PMC432822  PMID: 241077

Abstract

Crosslinking with dimethyl suberimidate reveals a chain of histone octamers in chromatin. The octamer can be isolated free in solution at high ionic strength and pH. The identification of dimers formed by crosslinking reveals two or more contacts of each histone with others within the octamer. The molecular weight (110,000) and pattern of dissociation of the octamer are compatible with the composition (F2A1)2(F3)2(F2A2)2(F2B)2.

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Selected References

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  1. Bonner W. M. Protein migration into nuclei. I. Frog oocyte nuclei in vivo accumulate microinjected histones, allow entry to small proteins, and exclude large proteins. J Cell Biol. 1975 Feb;64(2):421–430. doi: 10.1083/jcb.64.2.421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradbury E. M., Carpenter B. G., Rattle H. W. Magnetic resonance studies of deoxyribonucleoprotein. Nature. 1973 Jan 12;241(5385):123–126. doi: 10.1038/241123a0. [DOI] [PubMed] [Google Scholar]
  3. Burgoyne L. A., Hewish D. R., Mobbs J. Mammalian chromatin substructure studies with the calcium-magnesium endonuclease and two-dimensional polyacrylamide-gel electrophoresis. Biochem J. 1974 Oct;143(1):67–72. doi: 10.1042/bj1430067. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Clark V. M., Lilley D. M., Howarth O. W., Richards B. M., Pardon J. F. The structure and properties of histone F2a comprising the heterologous group F2a1 and F2a2 studied by 13C nuclear magnetic resonance. Nucleic Acids Res. 1974 Jul;1(7):865–880. doi: 10.1093/nar/1.7.865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. D'Anna J. A., Jr, Isenberg I. A complex of histones IIb2 and IV. Biochemistry. 1973 Mar 13;12(6):1035–1043. doi: 10.1021/bi00730a003. [DOI] [PubMed] [Google Scholar]
  6. D'Anna J. A., Jr, Isenberg I. A histone cross-complexing pattern. Biochemistry. 1974 Nov 19;13(24):4992–4997. doi: 10.1021/bi00721a019. [DOI] [PubMed] [Google Scholar]
  7. D'Anna J. A., Jr, Isenberg I. Interactions of histone LAK (f2a2) with histones KAS (f2b) and GRK (f2a1). Biochemistry. 1974 May 7;13(10):2098–2104. doi: 10.1021/bi00707a016. [DOI] [PubMed] [Google Scholar]
  8. Davies G. E., Stark G. R. Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc Natl Acad Sci U S A. 1970 Jul;66(3):651–656. doi: 10.1073/pnas.66.3.651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Griffith J. D. Chromatin structure: deduced from a minichromosome. Science. 1975 Mar 28;187(4182):1202–1203. doi: 10.1126/science.187.4182.1202. [DOI] [PubMed] [Google Scholar]
  10. Hyde J. E., Walker I. O. Covalent cross-linking of histones in chromatin. FEBS Lett. 1975 Feb 1;50(2):150–154. doi: 10.1016/0014-5793(75)80477-7. [DOI] [PubMed] [Google Scholar]
  11. Ilyin Y. V., Varshavsky A. Y., Mickelsaar U. N., Georgiev G. P. Studies on deoxyribonucleoprotein structure. Redistribution of proteins in mixtures of deoxyribonucleoproteins, DNA and RNA. Eur J Biochem. 1971 Sep 24;22(2):235–245. doi: 10.1111/j.1432-1033.1971.tb01537.x. [DOI] [PubMed] [Google Scholar]
  12. Kelley R. I. Isolation of a histone IIb1-IIb2 complex. Biochem Biophys Res Commun. 1973 Oct 15;54(4):1588–1594. doi: 10.1016/0006-291x(73)91168-6. [DOI] [PubMed] [Google Scholar]
  13. Kornberg R. D. Chromatin structure: a repeating unit of histones and DNA. Science. 1974 May 24;184(4139):868–871. doi: 10.1126/science.184.4139.868. [DOI] [PubMed] [Google Scholar]
  14. Kornberg R. D., Thomas J. O. Chromatin structure; oligomers of the histones. Science. 1974 May 24;184(4139):865–868. doi: 10.1126/science.184.4139.865. [DOI] [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Mirsky A. E., Burdick C. J., Davidson E. H., Littau V. C. The role of lysine-rich histone in the maintenance of chromatin structure in metaphase chromosomes. Proc Natl Acad Sci U S A. 1968 Oct;61(2):592–597. doi: 10.1073/pnas.61.2.592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Noll M. Subunit structure of chromatin. Nature. 1974 Sep 20;251(5472):249–251. doi: 10.1038/251249a0. [DOI] [PubMed] [Google Scholar]
  18. Noll M., Thomas J. O., Kornberg R. D. Preparation of native chromatin and damage caused by shearing. Science. 1975 Mar 28;187(4182):1203–1206. doi: 10.1126/science.187.4182.1203. [DOI] [PubMed] [Google Scholar]
  19. Ohlenbusch H. H., Olivera B. M., Tuan D., Davidson N. Selective dissociation of histones from calf thymus nucleoprotein. J Mol Biol. 1967 Apr 28;25(2):299–315. doi: 10.1016/0022-2836(67)90143-x. [DOI] [PubMed] [Google Scholar]
  20. Oudet P., Gross-Bellard M., Chambon P. Electron microscopic and biochemical evidence that chromatin structure is a repeating unit. Cell. 1975 Apr;4(4):281–300. doi: 10.1016/0092-8674(75)90149-x. [DOI] [PubMed] [Google Scholar]
  21. Roark D. E., Geoghegan T. E., Keller G. H. A two-subunit histone complex from calf thymus. Biochem Biophys Res Commun. 1974 Jul 24;59(2):542–547. doi: 10.1016/s0006-291x(74)80014-8. [DOI] [PubMed] [Google Scholar]
  22. Skandrani E., Mizon J., Sautière P., Biserte G. Etude de la fraction F2b des histones de thymus de veau. Biochimie. 1972;54(10):1267–1272. doi: 10.1016/s0300-9084(72)80067-1. [DOI] [PubMed] [Google Scholar]
  23. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  24. van der Westhuyzen D. R., von Holt C. A new procedure for the isolation and fractionation of histones. FEBS Lett. 1971 May 20;14(5):333–337. doi: 10.1016/0014-5793(71)80294-6. [DOI] [PubMed] [Google Scholar]

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