Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Commentary
  • Published:

A lasting marriage: histones and DNA tie a knot that is here to stay

Nature Reviews Genetics volume 8, page S23 (2007)Cite this article

Access through your institution
Buy or subscribe

DNA and protein have been together for a long time. Since the dawn of the DNA age, cells have had to handle information transactions with the long DNA poly-anion while preventing spurious electrostatic interactions and controlling its topology. The major eukaryotic innovation to tackle these problems has been the family of highly conserved and functional histone proteins.

In a typical eukaryotic cell, histones and DNA exist in a 1:1 mass ratio, and are organized into a fundamental repeating unit — the nucleosome — to form chromatin. Each nucleosome is composed of DNA wrapped around an octamer of the four core histones H2A, H2B, H3 and H4. This tight packaging, which is further helped by linker histones and other less-abundant proteins, produces condensed chromosomes that allow faithful segregation of the genetic material in dividing cells. Yet this close connection between histone and DNA is more than a marriage of convenience: histones are also crucial information carriers, containing epigenetic information that regulates the usage of the underlying DNA. This vision of the partnership took some time to emerge, however, as DNA held centre stage for several decades as the information bearer.

This is a preview of subscription content, access via your institution

Access options

Access through your institution

Buy this article

  • Purchase on SpringerLink
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Reference

  1. Stedman, E. & Stedman, E. Cell specificity of histones. Nature 166, 780–781 (1950).

    Article  CAS  Google Scholar 

  2. Allfrey, V. G., Faulkner, R. & Mirsky, A. E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl Acad. Sci. USA 51, 786–794 (1964).

    Article  CAS  Google Scholar 

  3. Panyim, S. & Chalkley, R. High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. Biophys. 130, 337–346 (1969).

    Article  CAS  Google Scholar 

  4. Solomon, M. J., Larsen, P. L. & Varshavsky, A. Mapping protein–DNA interactions in vivo with formaldehyde: evidence that histone H4 is retained on a highly transcribed gene. Cell 53, 937–947 (1988).

    Article  CAS  Google Scholar 

  5. Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell 129, 823–837 (2007).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. David Shechter and C. David Allis are at The Laboratory of Chromatin Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA. alliscd@rockefeller.edu,

    David Shechter & C. David Allis

Authors
  1. David Shechter
    View author publications

    Search author on:PubMed Google Scholar

  2. C. David Allis
    View author publications

    Search author on:PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Shechter, D., Allis, C. A lasting marriage: histones and DNA tie a knot that is here to stay. Nat Rev Genet 8 (Suppl 1), S23 (2007). https://doi.org/10.1038/nrg2249

Download citation

  • Published:

  • Issue date:

  • DOI: https://doi.org/10.1038/nrg2249

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing