Research Article

Cryo-EM Study of the Chromatin Fiber Reveals a Double Helix Twisted by Tetranucleosomal Units

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Science  25 Apr 2014:
Vol. 344, Issue 6182, pp. 376-380
DOI: 10.1126/science.1251413

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Double Helix, Doubled

Chromatin consists of genomic DNA packaged onto nucleosomes—double donut-shaped complexes of histone proteins. Roughly 150 base pairs of DNA are wrapped around each nucleosome with variable lengths of linker DNA in-between. Using cryogenic electron microscopy, Song et al. (p. 376; see the Perspective by Travers) determined the 11 angstrom–resolution structure of a 12-nucleosome string of DNA. The segment forms a 30-nanometer fiber structure, which is itself double-helical, like the DNA it packages.


The hierarchical packaging of eukaryotic chromatin plays a central role in transcriptional regulation and other DNA-related biological processes. Here, we report the 11-angstrom–resolution cryogenic electron microscopy (cryo-EM) structures of 30-nanometer chromatin fibers reconstituted in the presence of linker histone H1 and with different nucleosome repeat lengths. The structures show a histone H1-dependent left-handed twist of the repeating tetranucleosomal structural units, within which the four nucleosomes zigzag back and forth with a straight linker DNA. The asymmetric binding and the location of histone H1 in chromatin play a role in the formation of the 30-nanometer fiber. Our results provide mechanistic insights into how nucleosomes compact into higher-order chromatin fibers.

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