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Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation
I. Garcia-Saez, H. Menoni, R. Boopathi, MS. Shukla, L. Soueidan, M. Noirclerc-Savoye, A. Le Roy, DA. Skoufias, J. Bednar, A. Hamiche, D. Angelov, C. Petosa, S. Dimitrov,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Cell Press Free Archives
od 1997-12-01 do Před 1 rokem
Free Medical Journals
od 1997 do Před 1 rokem
Free Medical Journals
od 1997 do Před 1 rokem
Open Access Digital Library
od 1997-12-01
Elsevier Open Access Journals
od 1997-12-01 do 2023-06-15
Elsevier Open Archive Journals
od 1997-12-01 do Před 1 rokem
- MeSH
- DNA chemie genetika metabolismus MeSH
- elektronová kryomikroskopie MeSH
- Escherichia coli genetika metabolismus MeSH
- exprese genu MeSH
- genetické vektory chemie metabolismus MeSH
- histony chemie genetika metabolismus MeSH
- hydroxylový radikál chemie MeSH
- interakční proteinové domény a motivy MeSH
- klonování DNA MeSH
- konformace proteinů, alfa-helix MeSH
- konformace proteinů, beta-řetězec MeSH
- krystalografie rentgenová MeSH
- lidé MeSH
- molekulární modely MeSH
- multimerizace proteinu MeSH
- nukleozomy chemie metabolismus ultrastruktura MeSH
- osmolární koncentrace MeSH
- protein 1 vytvářející nukleozómy chemie genetika metabolismus MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Xenopus laevis MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Chromatin adopts a diversity of regular and irregular fiber structures in vitro and in vivo. However, how an array of nucleosomes folds into and switches between different fiber conformations is poorly understood. We report the 9.7 Å resolution crystal structure of a 6-nucleosome array bound to linker histone H1 determined under ionic conditions that favor incomplete chromatin condensation. The structure reveals a flat two-start helix with uniform nucleosomal stacking interfaces and a nucleosome packing density that is only half that of a twisted 30-nm fiber. Hydroxyl radical footprinting indicates that H1 binds the array in an on-dyad configuration resembling that observed for mononucleosomes. Biophysical, cryo-EM, and crosslinking data validate the crystal structure and reveal that a minor change in ionic environment shifts the conformational landscape to a more compact, twisted form. These findings provide insights into the structural plasticity of chromatin and suggest a possible assembly pathway for a 30-nm fiber.
Roumen Tsanev Institute of Molecular Biology Bulgarian Academy of Sciences Sofia Bulgaria
Université Grenoble Alpes CNRS CEA Institut de Biologie Structurale 38000 Grenoble France
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- $a Garcia-Saez, Isabel $u Université Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.
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- $a Structure of an H1-Bound 6-Nucleosome Array Reveals an Untwisted Two-Start Chromatin Fiber Conformation / $c I. Garcia-Saez, H. Menoni, R. Boopathi, MS. Shukla, L. Soueidan, M. Noirclerc-Savoye, A. Le Roy, DA. Skoufias, J. Bednar, A. Hamiche, D. Angelov, C. Petosa, S. Dimitrov,
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- $a Dimitrov, Stefan $u Université Grenoble Alpes, CNRS UMR 5309, INSERM U1209, Institute for Advanced Biosciences (IAB), Site Santé - Allée des Alpes, 38700 La Tronche, France; "Roumen Tsanev" Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia, Bulgaria. Electronic address: stefan.dimitrov@univ-grenoble-alpes.fr.
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