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TitleCryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units.
Journal, issue, pagesScience, Vol. 344, Issue 6182, Page 376-380, Year 2014
Publish dateApr 25, 2014
AuthorsFeng Song / Ping Chen / Dapeng Sun / Mingzhu Wang / Liping Dong / Dan Liang / Rui-Ming Xu / Ping Zhu / Guohong Li /
PubMed AbstractThe 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 ...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.
External linksScience / PubMed:24763583
MethodsEM (single particle)
Resolution11.0 - 25.0 Å
Structure data

EMDB-2600:
Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetra-nucleosomal units
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-2601:
Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetra-nucleosomal units
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-2602:
Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetra-nucleosomal units
Method: EM (single particle) / Resolution: 25.0 Å

Source
  • Xenopus laevis (African clawed frog)
  • Homo sapiens (human)
  • unidentified (others)

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