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. 1975 Mar 1;64(3):528–537. doi: 10.1083/jcb.64.3.528

Visualization of chromatin substructure: upsilon bodies

PMCID: PMC2109536  PMID: 1150743

Abstract

Spread chromatin fibers, from isolated eucaryotic nuclei, reveal linear arrays of spherical particles (upsilon bodies), about 70 A in diameter, connected by thin filaments about 15 A wide. These particles have been observed in freshly isolated nuclei from rat thymus, rat liver, and chicken erythrocytes. In addition, upsilon bodies can be visualized in preparations of isolated sheared chromatin, and in chromatin reconstructed from dissociating solvent conditions (i.e., high urea- NaCl concentration). As a criterion for perturbation of native chromatin structure low-angle X-ray diffraction patterns were obtained from nuclear pellets at different stages in the preparation of nuclei fro electron microscopy. These results suggest that the particulate (upsilon body) structures observed by electron microscopy may be closely related to the native configuration of chromatin.

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Selected References

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  1. AMES B. N., DUBIN D. T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem. 1960 Mar;235:769–775. [PubMed] [Google Scholar]
  2. ANDERSON N. G., WILBUR K. M. Studies on isolated cell components. IV. The effect of various solutions on the isolated rat liver nucleus. J Gen Physiol. 1952 May;35(5):781–796. doi: 10.1085/jgp.35.5.781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bekhor I., Kung G. M., Bonner J. Sequence-specific interaction of DNA and chromosomal protein. J Mol Biol. 1969 Jan;39(2):351–364. doi: 10.1016/0022-2836(69)90322-2. [DOI] [PubMed] [Google Scholar]
  4. Bram S., Ris H. On the structure of nucleohistone. J Mol Biol. 1971 Feb 14;55(3):325–336. doi: 10.1016/0022-2836(71)90321-4. [DOI] [PubMed] [Google Scholar]
  5. Brasch K., Seligy V. L., Setterfield G. Effects of low salt concentration on structural organization and template activity of chromatin in chicken erythrocyte nuclei. Exp Cell Res. 1971 Mar;65(1):61–72. doi: 10.1016/s0014-4827(71)80050-2. [DOI] [PubMed] [Google Scholar]
  6. Brutlag D., Schlehuber C., Bonner J. Properties of formaldehyde-treated nucleohistone. Biochemistry. 1969 Aug;8(8):3214–3218. doi: 10.1021/bi00836a013. [DOI] [PubMed] [Google Scholar]
  7. DuPraw E. J. Evidence for a 'folded-fibre' organization in human chromosomes. Nature. 1966 Feb 5;209(5023):577–581. doi: 10.1038/209577a0. [DOI] [PubMed] [Google Scholar]
  8. Gall J. G. Chromosome fibers studied by a spreading technique. Chromosoma. 1966;20(2):221–233. doi: 10.1007/BF00335209. [DOI] [PubMed] [Google Scholar]
  9. Hill W. E., Rossetti G. P., Van Holde K. E. Physical studies of ribosomes from Escherichia coli. J Mol Biol. 1969 Sep 14;44(2):263–277. doi: 10.1016/0022-2836(69)90174-0. [DOI] [PubMed] [Google Scholar]
  10. Huberman J. A. Structure of chromosome fibers and chromosomes. Annu Rev Biochem. 1973;42:355–378. doi: 10.1146/annurev.bi.42.070173.002035. [DOI] [PubMed] [Google Scholar]
  11. LUZZATI V., NICOLAUIEFF A. THE STRUCTURE OF NUCLEOHISTONES AND NUCLEOPROTAMINES. J Mol Biol. 1963 Aug;7:142–163. doi: 10.1016/s0022-2836(63)80043-1. [DOI] [PubMed] [Google Scholar]
  12. Lampert F. Coiled supercoiled DNA in critical point dried and thin sectioned human chromosome fibres. Nat New Biol. 1971 Dec 8;234(49):187–188. doi: 10.1038/newbio234187a0. [DOI] [PubMed] [Google Scholar]
  13. Li H. J. Thermal denaturation of nucleohistones--effects of formaldehyde reaction. Biopolymers. 1972;11(4):835–847. doi: 10.1002/bip.1972.360110408. [DOI] [PubMed] [Google Scholar]
  14. MASTER R. W. POSSIBLE SYNTHESIS OF POLYRIBONUCLEOTIDES OF KNOWN BASE-TRIPLET SEQUENCES. Nature. 1965 Apr 3;206:93–93. doi: 10.1038/206093b0. [DOI] [PubMed] [Google Scholar]
  15. Miller O. L., Jr, Beatty B. R. Portrait of a gene. J Cell Physiol. 1969 Oct;74(2 Suppl):225+–225+. doi: 10.1002/jcp.1040740424. [DOI] [PubMed] [Google Scholar]
  16. Miller O. L., Jr, Beatty B. R. Visualization of nucleolar genes. Science. 1969 May 23;164(3882):955–957. doi: 10.1126/science.164.3882.955. [DOI] [PubMed] [Google Scholar]
  17. Miller O. L., Jr, Hamkalo B. A., Thomas C. A., Jr Visualization of bacterial genes in action. Science. 1970 Jul 24;169(3943):392–395. doi: 10.1126/science.169.3943.392. [DOI] [PubMed] [Google Scholar]
  18. Olins D. E., Olins A. L. Model nucleohistones: the interaction of F1 and F2al histones with native T7 DNA. J Mol Biol. 1971 May 14;57(3):437–455. doi: 10.1016/0022-2836(71)90102-1. [DOI] [PubMed] [Google Scholar]
  19. Olins D. E., Olins A. L. Physical studies of isolated eucaryotic nuclei. J Cell Biol. 1972 Jun;53(3):715–736. doi: 10.1083/jcb.53.3.715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Olins D. E., Wright E. B. Glutaraldehyde fixation of isolated eucaryotic nuclei. Evidence for histone-histone proximity. J Cell Biol. 1973 Nov;59(2 Pt 1):304–317. doi: 10.1083/jcb.59.2.304. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. PHILPOT J. S., STANIER J. E. The choice of the suspension medium for rat-liver-cell nuclei. Biochem J. 1956 Jun;63(2):214–223. doi: 10.1042/bj0630214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pardon J. F., Wilkins M. H. A super-coil model for nucleohistone. J Mol Biol. 1972 Jul 14;68(1):115–124. doi: 10.1016/0022-2836(72)90267-7. [DOI] [PubMed] [Google Scholar]
  23. Pooley A. S., Pardon J. F., Richards B. M. The relation between the unit thread of chromosomes and isolated nucleohistone. J Mol Biol. 1974 Jan 5;85(4):533–549. doi: 10.1016/0022-2836(74)90314-3. [DOI] [PubMed] [Google Scholar]
  24. RIS H., MIRSKY A. E. The state of the chromosomes in the interphase nucleus. J Gen Physiol. 1949 Mar 20;32(4):489–502. doi: 10.1085/jgp.32.4.489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. 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]
  26. Ris H., Kubai D. F. Chromosome structure. Annu Rev Genet. 1970;4:263–294. doi: 10.1146/annurev.ge.04.120170.001403. [DOI] [PubMed] [Google Scholar]
  27. 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]
  28. Sanders L. A. Isolation and characterization of the non-histone chromosomal proteins of developing avian erythroid cells. Biochemistry. 1974 Jan 29;13(3):527–534. doi: 10.1021/bi00700a020. [DOI] [PubMed] [Google Scholar]
  29. Savitsky J. P., Stand F. A simple method for measuring ribonucleic acid content of preparations of deoxyribonucleic acid. Nature. 1965 Aug 14;207(998):758–759. doi: 10.1038/207758a0. [DOI] [PubMed] [Google Scholar]
  30. Shelton K. R., Neelin J. M. Nuclear residual proteins from goose erythroid cells and liver. Biochemistry. 1971 Jun 8;10(12):2342–2348. doi: 10.1021/bi00788a026. [DOI] [PubMed] [Google Scholar]
  31. Slayter H. S., Shih T. Y., Adler A. J., Fasman G. D. Electron microscopy and circular dichroism studies on chromatin. Biochemistry. 1972 Aug 1;11(16):3044–3054. doi: 10.1021/bi00766a016. [DOI] [PubMed] [Google Scholar]

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