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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
. 1976 Feb;73(2):505–509. doi: 10.1073/pnas.73.2.505

Analysis of subunit organization in chicken erythrocyte chromatin.

B R Shaw, T M Herman, R T Kovacic, G S Beaudreau, K E Van Holde
PMCID: PMC335938  PMID: 1061151

Abstract

Micrococcal nuclease digestion of intact chicken erythrocyte nuclei is shown to result in the formation of core nucleoprotein particles containing about 140 base pairs of DNA. These core particles, which are almost entirely devoid of histones f1 and f2c, are derived from transient nucleoprotein particles containing an average of approximately 180 base pairs of DNA. Oligomers of these latter particles may be isolated after brief nuclease digestion. The time course of digestion of these oligomers demonstrates the existence of "spacer" regions of more accessible DNA between core particles. Redigestion of purified monomer core nucleoprotein particles gives rise to both single-strand and double-strand DNA fragment patterns similar to those resulting from digestions of chromatin in situ. This observation indicates that the core particles we isolate are representative of nucleoprotein structures existing within the nucleus.

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Selected References

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

  1. Axel R. Cleavage of DNA in nuclei and chromatin with staphylococcal nuclease. Biochemistry. 1975 Jul;14(13):2921–2925. doi: 10.1021/bi00684a020. [DOI] [PubMed] [Google Scholar]
  2. Axel R., Melchior W., Jr, Sollner-Webb B., Felsenfeld G. Specific sites of interaction between histones and DNA in chromatin. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4101–4105. doi: 10.1073/pnas.71.10.4101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ballal N. R., Goldberg D. A., Busch H. Dissociation and reconstitution of chromatin without appreciable degradation of the proteins. Biochem Biophys Res Commun. 1975 Feb 17;62(4):972–982. doi: 10.1016/0006-291x(75)90418-0. [DOI] [PubMed] [Google Scholar]
  4. Boedtker H., Crkvenjakov R. B., Dewey K. F., Lanks K. Some properties of high molecular weight ribonucleic acid isolated from chick embryo polysomes. Biochemistry. 1973 Oct 23;12(22):4356–4360. doi: 10.1021/bi00746a009. [DOI] [PubMed] [Google Scholar]
  5. Clark R. J., Felsenfeld G. Structure of chromatin. Nat New Biol. 1971 Jan 27;229(4):101–106. doi: 10.1038/newbio229101a0. [DOI] [PubMed] [Google Scholar]
  6. Hewish D. R., Burgoyne L. A. Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease. Biochem Biophys Res Commun. 1973 May 15;52(2):504–510. doi: 10.1016/0006-291x(73)90740-7. [DOI] [PubMed] [Google Scholar]
  7. KIRBY K. S. ISOLATION AND CHARACTERIZATION OF RIBOSOMAL RIBONUCLEIC ACID. Biochem J. 1965 Jul;96:266–269. doi: 10.1042/bj0960266. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Langmore J. P., Wooley J. C. Chromatin architecture: investigation of a subunit of chromatin by dark field electron microscopy. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2691–2695. doi: 10.1073/pnas.72.7.2691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Loening U. E. The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresis. Biochem J. 1967 Jan;102(1):251–257. doi: 10.1042/bj1020251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lohr D., Van Holde K. E. Yeast chromatin subunit structure. Science. 1975 Apr 11;188(4184):165–166. doi: 10.1126/science.1090006. [DOI] [PubMed] [Google Scholar]
  12. Noll M. Internal structure of the chromatin subunit. Nucleic Acids Res. 1974 Nov;1(11):1573–1578. doi: 10.1093/nar/1.11.1573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Noll M. Subunit structure of chromatin. Nature. 1974 Sep 20;251(5472):249–251. doi: 10.1038/251249a0. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Olins A. L., Olins D. E. Spheroid chromatin units (v bodies). Science. 1974 Jan 25;183(4122):330–332. doi: 10.1126/science.183.4122.330. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Panyim S., Bilek D., Chalkley R. An electrophoretic comparison of vertebrate histones. J Biol Chem. 1971 Jul 10;246(13):4206–4215. [PubMed] [Google Scholar]
  18. Panyim S., Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys. 1969 Mar;130(1):337–346. doi: 10.1016/0003-9861(69)90042-3. [DOI] [PubMed] [Google Scholar]
  19. Rill R., Van Holde K. E. Properties of nuclease-resistant fragments of calf thymus chromatin. J Biol Chem. 1973 Feb 10;248(3):1080–1083. [PubMed] [Google Scholar]
  20. Sahasrabuddhe C. G., Van Holde K. E. The effect of trypsin on nuclease-resistant chromatin fragments. J Biol Chem. 1974 Jan 10;249(1):152–156. [PubMed] [Google Scholar]
  21. Shaw B. R., Corden J. L., Sahasrabuddhe C. G., Van Holde K. E. Chromatographic separation of chromatin subunits. Biochem Biophys Res Commun. 1974 Dec 23;61(4):1193–1198. doi: 10.1016/s0006-291x(74)80410-9. [DOI] [PubMed] [Google Scholar]
  22. Sollner-Webb B., Felsenfeld G. A comparison of the digestion of nuclei and chromatin by staphylococcal nuclease. Biochemistry. 1975 Jul;14(13):2915–2920. doi: 10.1021/bi00684a019. [DOI] [PubMed] [Google Scholar]
  23. Staynov D. Z., Pinder J. C., Gratzer W. B. Molecular weight determination of nucleic acids by gel electrophoresis in non-aqueous solution. Nat New Biol. 1972 Jan 26;235(56):108–110. doi: 10.1038/newbio235108a0. [DOI] [PubMed] [Google Scholar]
  24. Van Holde K. E., Sahasrabuddhe C. G., Shaw B. R. A model for particulate structure in chromatin. Nucleic Acids Res. 1974 Nov;1(11):1579–1586. doi: 10.1093/nar/1.11.1579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weintraub H., Van Lente F. Dissection of chromosome structure with trypsin and nucleases. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4249–4253. doi: 10.1073/pnas.71.10.4249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. van Bruggen E. F., Arnberg A. C., van Holde K. E., Sahasrabuddhe C. G., Shaw B. R. Electron microscopy of chromatin subunit particles. Biochem Biophys Res Commun. 1974 Oct 23;60(4):1365–1370. doi: 10.1016/0006-291x(74)90348-9. [DOI] [PubMed] [Google Scholar]

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