دورية أكاديمية
Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1
| العنوان: | Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1 |
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| المؤلفون: | Bednar, Jan, Garcia-Saez, Isabel, Boopathi, Ramachandran, Cutter, Amber R., Papai, Gabor, Reymer, Anna, 1983, 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 |
| المساهمون: | Göteborgs universitet, Naturvetenskapliga fakulteten, Institutionen för kemi och molekylärbiologi, Gothenburg University, Faculty of Sciences, Department of Chemistry and Molecular Biology |
| المصدر: | Molecular Cell. 66:384 |
| مصطلحات موضوعية: | Fysikalisk kemi, Physical Chemistry, Annan kemi, Other Chemistry Topics, Biokemi och molekylärbiologi, Biochemistry and Molecular Biology, chromatin, cryo-EM, histone H1, hydroxyl radical footprinting, linker histone, nucleosome, protein-DNA crosslinking, X-ray crystallography |
| الوصف: | © 2017 Elsevier Inc. 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. |
| الوصول الحر: | https://gup.ub.gu.se/publication/265824Test |
| قاعدة البيانات: | SwePub |
Full Text Finder | تدمد: | 10972765 10974164 |
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| DOI: | 10.1016/j.molcel.2017.04.012 |