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. 1993 Oct 11;21(20):4734–4738. doi: 10.1093/nar/21.20.4734

Nucleosomal structure at hyperacetylated loci probed in nuclei by DNA-histone crosslinking.

K K Ebralidse 1, T R Hebbes 1, A L Clayton 1, A W Thorne 1, C Crane-Robinson 1
PMCID: PMC331498  PMID: 8233821

Abstract

Chemically induced histone-DNA crosslinking in nuclei is used to monitor structural changes in chromosomal domains containing hyperacetylated histones. Core particles harbouring the crosslinks are immunofractionated with antibodies specific for acetylated histones. Crosslinking is revealed by gel separation of tryptic peptides from core histones that carry 32P-labelled residual nucleotide. The large number of DNA-histone crosslinks retained indicates that acetylated core histone tails are not totally displaced from the DNA. Changes in the patterns of crosslinked peptides imply a restructuring of hyperacetylated histone-DNA interactions at several points within the nucleosome. This demonstrates that a distinct conformational state is adopted in acetylated nucleosomes, known to be concentrated at transcriptionally active loci.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 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]
  2. Boulikas T., Wiseman J. M., Garrard W. T. Points of contact between histone H1 and the histone octamer. Proc Natl Acad Sci U S A. 1980 Jan;77(1):127–131. doi: 10.1073/pnas.77.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ebralidse K. K., Grachev S. A., Mirzabekov A. D. A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA. Nature. 1988 Jan 28;331(6154):365–367. doi: 10.1038/331365a0. [DOI] [PubMed] [Google Scholar]
  4. Ebralidse K. K., Mirzabekov A. D. One-domain interaction of histone H4 with nucleosomal core DNA is restricted to a narrow DNA segment. FEBS Lett. 1986 Jan 1;194(1):69–72. doi: 10.1016/0014-5793(86)80053-9. [DOI] [PubMed] [Google Scholar]
  5. Felsenfeld G. Chromatin as an essential part of the transcriptional mechanism. Nature. 1992 Jan 16;355(6357):219–224. doi: 10.1038/355219a0. [DOI] [PubMed] [Google Scholar]
  6. Gushchin D. Iu, Ebralidze K. K., Mirzabekov A. D. Struktura nukleosom. Lokalizatsiia vzaimodeistvuiushchikh s DNK uchstkov gistonov H2A i H2B s pomoshchiu DNK-belkovykh sshivok. Mol Biol (Mosk) 1991 Sep-Oct;25(5):1400–1411. [PubMed] [Google Scholar]
  7. Hebbes T. R., Thorne A. W., Clayton A. L., Crane-Robinson C. Histone acetylation and globin gene switching. Nucleic Acids Res. 1992 Mar 11;20(5):1017–1022. doi: 10.1093/nar/20.5.1017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hebbes T. R., Thorne A. W., Crane-Robinson C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 1988 May;7(5):1395–1402. doi: 10.1002/j.1460-2075.1988.tb02956.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Johnson L. M., Kayne P. S., Kahn E. S., Grunstein M. Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6286–6290. doi: 10.1073/pnas.87.16.6286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kornberg R. D., Lorch Y. Irresistible force meets immovable object: transcription and the nucleosome. Cell. 1991 Nov 29;67(5):833–836. doi: 10.1016/0092-8674(91)90354-2. [DOI] [PubMed] [Google Scholar]
  11. Langmore J. P., Paulson J. R. Low angle x-ray diffraction studies of chromatin structure in vivo and in isolated nuclei and metaphase chromosomes. J Cell Biol. 1983 Apr;96(4):1120–1131. doi: 10.1083/jcb.96.4.1120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lee D. Y., Hayes J. J., Pruss D., Wolffe A. P. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell. 1993 Jan 15;72(1):73–84. doi: 10.1016/0092-8674(93)90051-q. [DOI] [PubMed] [Google Scholar]
  13. Megee P. C., Morgan B. A., Mittman B. A., Smith M. M. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science. 1990 Feb 16;247(4944):841–845. doi: 10.1126/science.2106160. [DOI] [PubMed] [Google Scholar]
  14. Nacheva G. A., Guschin D. Y., Preobrazhenskaya O. V., Karpov V. L., Ebralidse K. K., Mirzabekov A. D. Change in the pattern of histone binding to DNA upon transcriptional activation. Cell. 1989 Jul 14;58(1):27–36. doi: 10.1016/0092-8674(89)90399-1. [DOI] [PubMed] [Google Scholar]
  15. Norton V. G., Imai B. S., Yau P., Bradbury E. M. Histone acetylation reduces nucleosome core particle linking number change. Cell. 1989 May 5;57(3):449–457. doi: 10.1016/0092-8674(89)90920-3. [DOI] [PubMed] [Google Scholar]
  16. Norton V. G., Marvin K. W., Yau P., Bradbury E. M. Nucleosome linking number change controlled by acetylation of histones H3 and H4. J Biol Chem. 1990 Nov 15;265(32):19848–19852. [PubMed] [Google Scholar]
  17. Oliva R., Bazett-Jones D. P., Locklear L., Dixon G. H. Histone hyperacetylation can induce unfolding of the nucleosome core particle. Nucleic Acids Res. 1990 May 11;18(9):2739–2747. doi: 10.1093/nar/18.9.2739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Park E. C., Szostak J. W. Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML. Mol Cell Biol. 1990 Sep;10(9):4932–4934. doi: 10.1128/mcb.10.9.4932. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Turner B. M. Histone acetylation and control of gene expression. J Cell Sci. 1991 May;99(Pt 1):13–20. doi: 10.1242/jcs.99.1.13. [DOI] [PubMed] [Google Scholar]
  20. Wu R. S., Panusz H. T., Hatch C. L., Bonner W. M. Histones and their modifications. CRC Crit Rev Biochem. 1986;20(2):201–263. doi: 10.3109/10409238609083735. [DOI] [PubMed] [Google Scholar]
  21. van Holde K. E., Lohr D. E., Robert C. What happens to nucleosomes during transcription? J Biol Chem. 1992 Feb 15;267(5):2837–2840. [PubMed] [Google Scholar]

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