The nucleosome core all wrapped up

Access through your institution Buy or subscribe For many years, biologists have been trying to understand how DNA is packaged into chromosomes. A breakthrough came in the 1970s when it was

established that all eukaryotic chromosomes consist of a regularly repeating protein-DNA complex called the nucleosome1. Each nucleosome consists of a protein octamer, made up of two copies

each of histones H2A, H2B, H3 and H4, which, together with the fifth histone, H1, organizes about 200 base pairs (bp) of DNA. Further organization involves the assembly of nucleosomes into

higher-order chromatin structures. On page 251of this issue, Luger _et al_.2 report the much awaited high-resolution structure of the nucleosome core particle. This landmark structure

confirms many of the expected features of the nucleosome core. But it also reveals some surprises. Importantly, it provides a structural basis for interpreting the many molecular mechanisms

that have evolved to regulate access to the DNA in chromatin. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe

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AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * MRC Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge<, UK Daniela Rhodes Authors * Daniela Rhodes View author publications You

can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Rhodes, D. The nucleosome core all wrapped up.

_Nature_ 389, 231–232 (1997). https://doi.org/10.1038/38386 Download citation * Issue Date: 18 September 1997 * DOI: https://doi.org/10.1038/38386 SHARE THIS ARTICLE Anyone you share the

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