XB-ART-53990
Mol Cell
2017 May 04;663:384-397.e8. doi: 10.1016/j.molcel.2017.04.012.
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Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1.
Bednar J
,
Garcia-Saez I
,
Boopathi R
,
Cutter AR
,
Papai G
,
Reymer A
,
Syed SH
,
Lone IN
,
Tonchev O
,
Crucifix C
,
Menoni H
,
Papin C
,
Skoufias DA
,
Kurumizaka H
,
Lavery R
,
Hamiche A
,
Hayes JJ
,
Schultz P
,
Angelov D
,
Petosa C
,
Dimitrov S
.
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Linker histones associate with nucleosomes to promote the formation of higher-order chromatin structure, but the underlying molecular details are unclear. We investigated the structure of a 197 bp nucleosome bearing symmetric 25 bp linker DNA arms in complex with vertebrate linker histone H1. We determined electron cryo-microscopy (cryo-EM) and crystal structures of unbound and H1-bound nucleosomes and validated these structures by site-directed protein cross-linking and hydroxyl radical footprinting experiments. Histone H1 shifts the conformational landscape of the nucleosome by drawing the two linkers together and reducing their flexibility. The H1 C-terminal domain (CTD) localizes primarily to a single linker, while the H1 globular domain contacts the nucleosome dyad and both linkers, associating more closely with the CTD-distal linker. These findings reveal that H1 imparts a strong degree of asymmetry to the nucleosome, which is likely to influence the assembly and architecture of higher-order structures.
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Species referenced: Xenopus laevis
Genes referenced: kidins220
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