Stability of the Primary Organization of Nucleosome Core Particles Upon Some Conformational Transitions

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1981 Mar 11

PMID 7232210

Citations 5

Authors

V W Zayetz

S G Bavykin

V L Karpov

A D Mirzabekov

Affiliations

Soon will be listed here.

Abstract

The sequential arrangement of histones along DNA in nucleosome core particles was determined between 0.5 and 600 mM salt and from 0 to 8 M urea. These concentrations of salt and urea up to 6 M had no significant effect on the linear order of histones along DNA but 8 M urea caused the rearrangement of histones. Conformational changes in cores have been identified within these ranges of conditions by several laboratories 8-21. Also, abrupt structural changes in the cores, apparently their unfolding, were found by gel electrophoresis to occur at urea concentration, between 4 and 5 M. 600 mM salt and 6 M urea were shown to relax the binding of histones to DNA in cores but do not however release histones or some part of their molecules from DNA. It appears therefore that nucleosomal cores can undergo some conformational transitions and unfolding whereas their primary organization remains essentially unaffected. These results are consistent with a model of the core particles in which the histone octamer forms something like a helical "rim" along the superhelical DNA and histone-histone interactions beyond the "rim" are rather weak in comparison with those within the "rim".

Citing Articles

Microfluorometric investigations of chromatin structure. II. Mordant fluorochroming with ions that complex with morin.

COWDEN R, Curtis S Histochemistry. 1981; 72(3):391-400.

PMID: 6795151 DOI: 10.1007/BF00501781.

The chromatin structure of an actively expressed, single copy yeast gene.

Lohr D Nucleic Acids Res. 1983; 11(19):6755-73.

PMID: 6314257 PMC: 326412. DOI: 10.1093/nar/11.19.6755.

Primary organization of nucleosomal core particles is invariable in repressed and active nuclei from animal, plant and yeast cells.

Bavykin S, Usachenko S, Lishanskaya A, Shick V, Belyavsky A, Undritsov I Nucleic Acids Res. 1985; 13(10):3439-59.

PMID: 4011430 PMC: 341251. DOI: 10.1093/nar/13.10.3439.

ATP as an alternative inhibitor of bacterial and endogenous nucleases and its effect on native chromatin compaction.

Rosenberg N Mol Cell Biochem. 1987; 76(2):113-21.

PMID: 3118182 DOI: 10.1007/BF00223476.

Laser-induced crosslinking of histones to DNA in chromatin and core particles: implications in studying histone-DNA interactions.

Stefanovsky VYu , Dimitrov S, Russanova V, Angelov D, Pashev I Nucleic Acids Res. 1989; 17(23):10069-81.

PMID: 2602113 PMC: 335231. DOI: 10.1093/nar/17.23.10069.

References

GLOVER J, Salter D, Shepherd B . A study of some factors that influence the iodination of ox insulin. Biochem J. 1967; 103(1):120-8. PMC: 1270376. DOI: 10.1042/bj1030120. View

Creighton T . Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J Mol Biol. 1980; 137(1):61-80. DOI: 10.1016/0022-2836(80)90157-6. View

Elgin S, HOOD L . Chromosomal proteins of Drosophila embryos. Biochemistry. 1973; 12(24):4984-91. DOI: 10.1021/bi00748a026. View

Varshavsky A, Bakayev V, Georgiev G . Heterogeneity of chromatin subunits in vitro and location of histone H1. Nucleic Acids Res. 1976; 3(2):477-92. PMC: 342917. DOI: 10.1093/nar/3.2.477. View

Yaneva M, Dessev G . Persistence of the ten-nucleotide repeat in chromatin unfolded in urea, as revealed by digestion with deoxyribonuclease i. Nucleic Acids Res. 1976; 3(7):1761-7. PMC: 343034. DOI: 10.1093/nar/3.7.1761. View

Weintraub H, WORCEL A, Alberts B . A model for chromatin based upon two symmetrically paired half-nucleosomes. Cell. 1976; 9(3):409-17. DOI: 10.1016/0092-8674(76)90085-4. View

Finch J, Lutter L, Rhodes D, Brown R, Rushton B, Levitt M . Structure of nucleosome core particles of chromatin. Nature. 1977; 269(5623):29-36. DOI: 10.1038/269029a0. View

Olins D, Bryan P, Harrington R, Hill W, Olins A . Conformational states of chromatin nu bodies induced by urea. Nucleic Acids Res. 1977; 4(6):1911-31. PMC: 342531. DOI: 10.1093/nar/4.6.1911. View

Pardon J, Worcester D, Wooley J, Cotter R, Lilley D, RICHARDS R . The structure of the chromatin core particle in solution. Nucleic Acids Res. 1977; 4(9):3199-214. PMC: 342644. DOI: 10.1093/nar/4.9.3199. View

10.

Hardison R, Zeitler D, Murphy J, Chalkley R . Histone neighbors in nuclei and extended chromatin. Cell. 1977; 12(2):417-27. DOI: 10.1016/0092-8674(77)90118-0. View

11.

Suau P, Kneale G, Braddock G, Baldwin J, Bradbury E . A low resolution model for the chromatin core particle by neutron scattering. Nucleic Acids Res. 1977; 4(11):3769-86. PMC: 343199. DOI: 10.1093/nar/4.11.3769. View

12.

Gordon V, Knobler C, Olins D, Schumaker V . Conformational changes of the chromatin subunit. Proc Natl Acad Sci U S A. 1978; 75(2):660-3. PMC: 411315. DOI: 10.1073/pnas.75.2.660. View

13.

Trifonov E . The helical model of the nucleosome core. Nucleic Acids Res. 1978; 5(4):1371-80. PMC: 342084. DOI: 10.1093/nar/5.4.1371. View

14.

Woodcock C, Frado L . Ultrastructure of chromatin subunits during unfolding, histone depletion, and reconstitution. Cold Spring Harb Symp Quant Biol. 1978; 42 Pt 1:43-55. DOI: 10.1101/sqb.1978.042.01.007. View

15.

Cary P, Moss T, Bradbury E . High-resolution proton-magnetic-resonance studies of chromatin core particles. Eur J Biochem. 1978; 89(2):475-82. DOI: 10.1111/j.1432-1033.1978.tb12551.x. View

16.

Wong N, Candido E . Histone H3 thiol reactivity as a probe of nucleosome structure. J Biol Chem. 1978; 253(22):8263-8. View

17.

Martinson H, True R, Burch J . Specific histone-histone contacts are ruptured when nucleosomes unfold at low ionic strength. Biochemistry. 1979; 18(6):1082-9. DOI: 10.1021/bi00573a023. View

18.

Martinson H, True R . On the mechanism of nucleosome unfolding. Biochemistry. 1979; 18(6):1089-94. DOI: 10.1021/bi00573a024. View

19.

PRUNELL A, Kornberg R, Lutter L, Klug A, Levitt M, Crick F . Periodicity of deoxyribonuclease I digestion of chromatin. Science. 1979; 204(4395):855-8. DOI: 10.1126/science.441739. View

20.

Dieterich A, Axel R, Cantor C . Salt-induced structural changes of nucleosome core particles. J Mol Biol. 1979; 129(4):587-602. DOI: 10.1016/0022-2836(79)90470-4. View