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. 1985 Dec 16;4(13A):3455–3462. doi: 10.1002/j.1460-2075.1985.tb04104.x

The arrangement of H5 molecules in extended and condensed chicken erythrocyte chromatin.

A C Lennard, J O Thomas
PMCID: PMC554684  PMID: 4092684

Abstract

Chemical cross-linking with dithiobis(succinimidyl propionate) has been used to investigate the relative disposition of neighbouring H5 (H1) molecules in chicken erythrocyte chromatin in the extended (nucleosome filament) and condensed (300 A filament) states; in this chromatin H5 and H1 are interspersed along the nucleosome filament, rather than segregated into blocks, as shown by the nature of the cross-linked dimers and their relative amounts. Detailed analysis of the cross-linked H5 homopolymers from extended chromatin and condensed nuclear chromatin indicates which domains of H5 are in contact (or close proximity) in the two states. Two results suggest a polar, head-to-tail arrangement of H5 molecules along the nucleosome filament. This arrangement persists when chromatin adopts higher-order structure but in the folded state neighbouring basic C-terminal domains, in particular, are more closely juxtaposed than they are in extended chromatin.

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Selected References

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  1. Allan J., Hartman P. G., Crane-Robinson C., Aviles F. X. The structure of histone H1 and its location in chromatin. Nature. 1980 Dec 25;288(5792):675–679. doi: 10.1038/288675a0. [DOI] [PubMed] [Google Scholar]
  2. Aviles F. J., Chapman G. E., Kneale G. G., Crane-Robinson C., Bradbury E. M. The conformation of histone H5. Isolation and characterisation of the globular segment. Eur J Biochem. 1978 Aug 1;88(2):363–371. doi: 10.1111/j.1432-1033.1978.tb12457.x. [DOI] [PubMed] [Google Scholar]
  3. Bates D. L., Butler P. J., Pearson E. C., Thomas J. O. Stability of the higher-order structure of chicken-erythrocyte chromatin in solution. Eur J Biochem. 1981 Oct;119(3):469–476. doi: 10.1111/j.1432-1033.1981.tb05631.x. [DOI] [PubMed] [Google Scholar]
  4. Bates D. L., Thomas J. O. Histones H1 and H5: one or two molecules per nucleosome? Nucleic Acids Res. 1981 Nov 25;9(22):5883–5894. doi: 10.1093/nar/9.22.5883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bradbury E. M., Chapman G. E., Danby S. E., Hartman P. G., Riches P. L. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The properties of the N-terminal and C-terminal halves of histone H1. Eur J Biochem. 1975 Sep 15;57(2):521–528. doi: 10.1111/j.1432-1033.1975.tb02327.x. [DOI] [PubMed] [Google Scholar]
  6. Briand G., Kmiecik D., Sautiere P., Wouters D., Borie-Loy O., Biserte G., Mazen A., Champagne M. Chicken erythrocyte histone H5. IV. Sequence of the carboxy-termined half of the molecule (96 residues) and complete sequence. FEBS Lett. 1980 Apr 7;112(2):147–151. doi: 10.1016/0014-5793(80)80167-0. [DOI] [PubMed] [Google Scholar]
  7. Butler P. J., Thomas J. O. Changes in chromatin folding in solution. J Mol Biol. 1980 Jul 15;140(4):505–529. doi: 10.1016/0022-2836(80)90268-5. [DOI] [PubMed] [Google Scholar]
  8. Camerini-Otero R. D., Sollner-Webb B., Felsenfeld G. The organization of histones and DNA in chromatin: evidence for an arginine-rich histone kernel. Cell. 1976 Jul;8(3):333–347. doi: 10.1016/0092-8674(76)90145-8. [DOI] [PubMed] [Google Scholar]
  9. Finch J. T., Klug A. Solenoidal model for superstructure in chromatin. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1897–1901. doi: 10.1073/pnas.73.6.1897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hayashi K., Hofstaetter T., Yakuwa N. Asymmetry of chromatin subunits probed with histone H1 in an H1-DNA complex. Biochemistry. 1978 May 16;17(10):1880–1883. doi: 10.1021/bi00603a012. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lomant A. J., Fairbanks G. Chemical probes of extended biological structures: synthesis and properties of the cleavable protein cross-linking reagent [35S]dithiobis(succinimidyl propionate). J Mol Biol. 1976 Jun 14;104(1):243–261. doi: 10.1016/0022-2836(76)90011-5. [DOI] [PubMed] [Google Scholar]
  14. NEELIN J. M., CALLAHAN P. X., LAMB D. C., MURRAY K. THE HISTONES OF CHICKEN ERYTHROCYTE NUCLEI. Can J Biochem. 1964 Dec;42:1743–1752. doi: 10.1139/o64-185. [DOI] [PubMed] [Google Scholar]
  15. Nelson P. P., Albright S. C., Wiseman J. M., Garrard W. T. Reassociation of histone H1 with nucleosomes. J Biol Chem. 1979 Nov 25;254(22):11751–11760. [PubMed] [Google Scholar]
  16. Nikolaev L. G., Glotov B. O., Dashkevich V. K., Barbashov S. F., Severin E. S. Mutual arrangement of histone H1 molecules in extended chromatin. Chymotryptic digestion of cross-linked H1 histone dimers. FEBS Lett. 1983 Oct 31;163(1):66–68. doi: 10.1016/0014-5793(83)81164-8. [DOI] [PubMed] [Google Scholar]
  17. Nikolaev L. G., Glotov B. O., Itkes A. V., Severin E. S. Mutual arrangement of histone H1 molecules in chromatin of intact nuclei. FEBS Lett. 1981 Mar 9;125(1):20–24. doi: 10.1016/0014-5793(81)80987-8. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Pearson E. C., Butler P. J., Thomas J. O. Higher-order structure of nucleosome oligomers from short-repeat chromatin. EMBO J. 1983;2(8):1367–1372. doi: 10.1002/j.1460-2075.1983.tb01593.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pospelov V. A., Jerkin A. M., Khachatrian A. T. H1 and H5 histone arrangement in chromatin of pigeon erythrocytes. FEBS Lett. 1981 Jun 15;128(2):315–317. doi: 10.1016/0014-5793(81)80106-8. [DOI] [PubMed] [Google Scholar]
  21. Ring D., Cole R. D. Close contacts between H1 histone molecules in nuclei. J Biol Chem. 1983 Dec 25;258(24):15361–15364. [PubMed] [Google Scholar]
  22. SANGER F., THOMPSON E. O. Halogenation of tyrosine during acid hydrolysis. Biochim Biophys Acta. 1963 May 14;71:468–471. doi: 10.1016/0006-3002(63)91108-9. [DOI] [PubMed] [Google Scholar]
  23. Sugarman B. J., Dodgson J. B., Engel J. D. Genomic organization, DNA sequence, and expression of chicken embryonic histone genes. J Biol Chem. 1983 Jul 25;258(14):9005–9016. [PubMed] [Google Scholar]
  24. Thomas J. O., Khabaza A. J. Cross-linking of histone H1 in chromatin. Eur J Biochem. 1980 Dec;112(3):501–511. doi: 10.1111/j.1432-1033.1980.tb06113.x. [DOI] [PubMed] [Google Scholar]
  25. Thomas J. O., Kornberg R. D. The study of histone--histone associations by chemical cross-linking. Methods Cell Biol. 1978;18:429–440. [PubMed] [Google Scholar]
  26. Thomas J. O., Rees C. Exchange of histones H1 and H5 between chromatin fragments. A preference of H5 for higher-order structures. Eur J Biochem. 1983 Jul 15;134(1):109–115. doi: 10.1111/j.1432-1033.1983.tb07538.x. [DOI] [PubMed] [Google Scholar]
  27. Torres-Martinez S., Ruiz-Carrillo A. Nucleosomes containing histones H1 or H5 are closely interspersed in chromatin. Nucleic Acids Res. 1982 Apr 10;10(7):2323–2335. doi: 10.1093/nar/10.7.2323. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wray W., Boulikas T., Wray V. P., Hancock R. Silver staining of proteins in polyacrylamide gels. Anal Biochem. 1981 Nov 15;118(1):197–203. doi: 10.1016/0003-2697(81)90179-2. [DOI] [PubMed] [Google Scholar]

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