Rearrangement of the histone H2A C-terminal domain in the nucleosome - PubMed (original) (raw)

Rearrangement of the histone H2A C-terminal domain in the nucleosome

S I Usachenko et al. Proc Natl Acad Sci U S A. 1994.

Abstract

Using zero-length covalent protein-DNA crosslinking, we have mapped the histone-DNA contacts in nucleosome core particles from which the C- and N-terminal domains of histone H2A were selectively trimmed by trypsin or clostripain. We found that the flexible trypsin-sensitive C-terminal domain of histone H2A contacts the dyad axis, whereas its globular domain contacts the end of DNA in the nucleosome core particle. The appearance of the histone H2A contact at the dyad axis occurs only in the absence of linker DNA and does not depend on the absence of linker histones. Our results show the ability of the histone H2A C-terminal domain to rearrange. This rearrangement might play a biological role in nucleosome disassembly and reassembly and the retention of the H2A-H2B dimer (or the whole octamer) during the passing of polymerases through the nucleosome.

PubMed Disclaimer

Similar articles

• Structural basis for ATP-dependent chromatin remodelling by the INO80 complex.
  Eustermann S, Schall K, Kostrewa D, Lakomek K, Strauss M, Moldt M, Hopfner KP. Eustermann S, et al. Nature. 2018 Apr;556(7701):386-390. doi: 10.1038/s41586-018-0029-y. Epub 2018 Apr 11. Nature. 2018. PMID: 29643509 Free PMC article.
• Core histone-DNA interactions in sea urchin sperm chromatin. The N-terminal tail of H2B interacts with linker DNA.
  Hill CS, Thomas JO. Hill CS, et al. Eur J Biochem. 1990 Jan 12;187(1):145-53. doi: 10.1111/j.1432-1033.1990.tb15288.x. Eur J Biochem. 1990. PMID: 2298202
• Nucleosome adaptability conferred by sequence and structural variations in histone H2A-H2B dimers.
  Shaytan AK, Landsman D, Panchenko AR. Shaytan AK, et al. Curr Opin Struct Biol. 2015 Jun;32:48-57. doi: 10.1016/j.sbi.2015.02.004. Epub 2015 Feb 27. Curr Opin Struct Biol. 2015. PMID: 25731851 Free PMC article. Review.
• Histone-DNA contacts in structure/function relationships of nucleosomes as revealed by crosslinking.
  Usachenko SI, Bradbury EM. Usachenko SI, et al. Genetica. 1999;106(1-2):103-15. doi: 10.1023/a:1003785031470. Genetica. 1999. PMID: 10710716 Review.

Cited by

• The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.
  Cavalieri V. Cavalieri V. Genes (Basel). 2021 Oct 10;12(10):1596. doi: 10.3390/genes12101596. Genes (Basel). 2021. PMID: 34680990 Free PMC article. Review.
• The dark side of histones: genomic organization and role of oncohistones in cancer.
  Amatori S, Tavolaro S, Gambardella S, Fanelli M. Amatori S, et al. Clin Epigenetics. 2021 Apr 7;13(1):71. doi: 10.1186/s13148-021-01057-x. Clin Epigenetics. 2021. PMID: 33827674 Free PMC article. Review.
• Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization.
  Shakya A, Park S, Rana N, King JT. Shakya A, et al. Biophys J. 2020 Feb 4;118(3):753-764. doi: 10.1016/j.bpj.2019.12.022. Epub 2019 Dec 31. Biophys J. 2020. PMID: 31952807 Free PMC article.
• Distinct Roles of Histone H3 and H2A Tails in Nucleosome Stability.
  Li Z, Kono H. Li Z, et al. Sci Rep. 2016 Aug 16;6:31437. doi: 10.1038/srep31437. Sci Rep. 2016. PMID: 27527579 Free PMC article.
• Subnucleosomal structures and nucleosome asymmetry across a genome.
  Rhee HS, Bataille AR, Zhang L, Pugh BF. Rhee HS, et al. Cell. 2014 Dec 4;159(6):1377-88. doi: 10.1016/j.cell.2014.10.054. Cell. 2014. PMID: 25480300 Free PMC article.

References

1. 1. Cell. 1989 Jul 14;58(1):27-36 - PubMed
2. 1. J Mol Biol. 1989 Apr 5;206(3):451-63 - PubMed
3. 1. J Mol Biol. 1990 Apr 5;212(3):495-511 - PubMed
4. 1. Proc Natl Acad Sci U S A. 1990 Aug;87(15):5724-8 - PubMed
5. 1. J Mol Biol. 1991 Apr 20;218(4):805-13 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Atypon
  • Europe PubMed Central
  • PubMed Central