Small angle neutron scattering studies of chromatin subunits in solution
- PMID: 556978
- DOI: 10.1016/0092-8674(77)90148-9
Small angle neutron scattering studies of chromatin subunits in solution
Abstract
Neutron scattering studies have been performed on dilute solutions of the fundamental subunit of chromatin, the nucleosome. The subunits contain approximately 195 base paris (bp) of DNA and histones H2A, H2B, H3, and H4. Measurements of the small angle scattering curves in various H2O/D2O solvents allow the contrast dependence of the radius of gyration of the subunits to be examined and give the mean scattering density of the particle. Further application of contrast variation to the higher angle scatter curves allows the contributions from the shape and internal structure of the subunits to be analyzed separately. From these results, we are able to propose a spherically averaged structure with most of the histones closely packed into a core of radius 3.2 nm surrounded by a loosely packed DNA-rich shell of 2.0 nm thickness resulting in a particle of 5.2 nm average radius. Model calculations for ellipsoids show that the outer shape of the subunit must have an axial ratio between 0.5 and 1.4 but is probably best described by more spherical particle. These results are correlated with the diffraction from chromatin films to provide an explanation for some of the diffraction rings.
Similar articles
-
Low-angle neutron scattering from chromatin subunit particles.Nucleic Acids Res. 1975 Nov;2(11):2163-76. doi: 10.1093/nar/2.11.2163. Nucleic Acids Res. 1975. PMID: 1052536 Free PMC article.
-
A low resolution model for the chromatin core particle by neutron scattering.Nucleic Acids Res. 1977 Nov;4(11):3769-86. doi: 10.1093/nar/4.11.3769. Nucleic Acids Res. 1977. PMID: 593885 Free PMC article.
-
Neutron scattering studies of the H2a-H2b and (H3-H4)2 histone complexes.Basic Life Sci. 1984;27:47-72. doi: 10.1007/978-1-4899-0375-4_3. Basic Life Sci. 1984. PMID: 6712573
-
Utilization of neutron scattering for analysis of chromatin and nucleoprotein structure.Methods Cell Biol. 1978;18:295-325. doi: 10.1016/s0091-679x(08)60144-2. Methods Cell Biol. 1978. PMID: 355791 Review. No abstract available.
-
Neutron scattering studies of biological macromolecules in solution.Q Rev Biophys. 1977 Nov;10(4):485-527. doi: 10.1017/s0033583500003206. Q Rev Biophys. 1977. PMID: 343153 Review. No abstract available.
Cited by
-
The superstructure of chromatin and its condensation mechanism. I. Synchrotron radiation X-ray scattering results.Eur Biophys J. 1986;13(3):157-73. doi: 10.1007/BF00542560. Eur Biophys J. 1986. PMID: 3956445
-
The internal organization of mycobacterial partition assembly: does the DNA wrap a protein core?PLoS One. 2012;7(12):e52690. doi: 10.1371/journal.pone.0052690. Epub 2012 Dec 20. PLoS One. 2012. PMID: 23285150 Free PMC article.
-
In vitro core particle and nucleosome assembly at physiological ionic strength.Proc Natl Acad Sci U S A. 1979 Jul;76(7):3284-8. doi: 10.1073/pnas.76.7.3284. Proc Natl Acad Sci U S A. 1979. PMID: 291002 Free PMC article.
-
Nucleosome mono, di, tri-, and tetramers from chicken embryo chromatin.Nucleic Acids Res. 1977 Nov;4(11):3901-17. doi: 10.1093/nar/4.11.3901. Nucleic Acids Res. 1977. PMID: 593894 Free PMC article.
-
On the biological role of histone acetylation.Biochem J. 1990 Jan 1;265(1):23-38. doi: 10.1042/bj2650023. Biochem J. 1990. PMID: 2405837 Free PMC article. Review. No abstract available.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources