Details

Autor(en) / Beteiligte

• Bednar, Jan
• Garcia-Saez, Isabel
• Boopathi, Ramachandran
• Cutter, Amber R.
• Papai, Gabor
• Reymer, Anna
• Syed, Sajad H.
• Lone, Imtiaz Nisar
• Tonchev, Ognyan
• Crucifix, Corinne
• Menoni, Hervé
• Papin, Christophe
• Skoufias, Dimitrios A.
• Kurumizaka, Hitoshi
• Lavery, Richard
• Hamiche, Ali
• Hayes, Jeffrey J.
• Schultz, Patrick
• Angelov, Dimitar
• Petosa, Carlo
• Dimitrov, Stefan

Titel

Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1

Ist Teil von

• Molecular cell, 2017-05, Vol.66 (3), p.384-397.e8

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2017

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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. [Display omitted] •Cryo-EM and crystal structures of the nucleosome bound to histone H1 were determined•H1 binding induces the nucleosome to adopt a more compact and rigid conformation•The H1 globular domain interacts with core DNA on the dyad and with both DNA linkers•The H1 C-terminal domain associates primarily with a single DNA linker Bednar et al. report cryo-EM and crystal structures of a 197 bp nucleosome bound to histone H1, revealing that H1 stabilizes a compact nucleosome conformation. The H1 globular domain binds on the nucleosome dyad, while the C-terminal domain localizes primarily to a single DNA linker, conferring polarity to the nucleosome.