Abstract
There is considerable current interest in the organisation of nucleosomes in chromatin. A strong X-ray and neutron semi-meridional diffraction peak at approximately 10 nm had previously been attributed to the interparticle specing of a linear array of nucleosomes. This diffraction peak could also result from a close packed helical array of nucleosomes. A direct test of these proposals is whether the 10 nm peak is truly meridional as would be expected for a linear array of nucleosomes or is slightly off the meridian as expected for a helical array. Neutron diffraction studies of H1-depleted chromatin support the latter alternative. The 10 nm peak has maxima which form a cross-pattern with semi-meridional angle of 8 to 9 degrees. This is consistent with a coil of nucleosomes of pitch 10 nm and outer diameter of approximately 30 nm. These dimensions correspond to about six nucleosomes per turn of the coli.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Baldwin J. P., Boseley P. G., Bradbury E. M., Ibel K. The subunit structure of the eukaryotic chromosome. Nature. 1975 Jan 24;253(5489):245–249. doi: 10.1038/253245a0. [DOI] [PubMed] [Google Scholar]
- 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]
- Bradbury E. M., Cary P. D., Crane-Robinson C., Rattle H. W., Boublik M., Sautière P. Conformations and interactions of histone H2A (F2A2, ALK). Biochemistry. 1975 May 6;14(9):1876–1885. doi: 10.1021/bi00680a012. [DOI] [PubMed] [Google Scholar]
- Bradbury E. M., Molgaard H. V., Stephens R. M., Bolund L. A., Johns E. W. X-ray studies of nucleoproteins depleted of lysine-rich histone. Eur J Biochem. 1972 Dec 18;31(3):474–482. doi: 10.1111/j.1432-1033.1972.tb02555.x. [DOI] [PubMed] [Google Scholar]
- Bradbury E. M., Rattle H. W. Simple computer-aided approach for the analyses of the nuclear-magnetic-resonance spectra of histones. Fractions F1, Fsa1, F2B, cleaved halves of F2B and F2B-DNA. Eur J Biochem. 1972 May 23;27(2):270–281. doi: 10.1111/j.1432-1033.1972.tb01836.x. [DOI] [PubMed] [Google Scholar]
- Carlson R. D., Olins D. E. Chromatin model calculations: Arrays of spherical nu bodies. Nucleic Acids Res. 1976 Jan;3(1):89–100. doi: 10.1093/nar/3.1.89. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- Pardon J. F., Worcester D. L., Wooley J. C., Tatchell K., Van Holde K. E., Richards B. M. Low-angle neutron scattering from chromatin subunit particles. Nucleic Acids Res. 1975 Nov;2(11):2163–2176. doi: 10.1093/nar/2.11.2163. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]