Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-49796
Science 2014 Apr 25;3446182:376-80. doi: 10.1126/science.1251413.
Show Gene links Show Anatomy links

Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units.

Song F , Chen P , Sun D , Wang M , Dong L , Liang D , Xu RM , Zhu P , Li G .


???displayArticle.abstract???
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.

???displayArticle.pubmedLink??? 24763583
???displayArticle.link??? Science


Species referenced: Xenopus laevis
Genes referenced: twist1

References :
Travers, Structural biology. The 30-nm fiber redux. 2014, Pubmed