Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
| Autor: | Sara Sandin, Nikolay Korolev, Lars Nordenskiöld, Nikolay V. Berezhnoy, Chun-Jen Su, Aghil Soman, Sai Wang, Zhehui Barry Liu, Andrew S.W. Wong, Vinod Kumar Vogirala |
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| Přispěvatelé: | School of Biological Sciences, NTU Institute of Structural Biology, Singapore Center for Environmental Life Sciences Engineering |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Models Molecular Science Chromatin structure Article Histones 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine X-Ray Diffraction Scattering Small Angle Nucleosome Humans Protein Structure Quaternary Chromatin Structure Multidisciplinary biology Base Sequence Small-angle X-ray scattering Biological sciences [Science] DNA Linker DNA Chromatin Nucleosomes 030104 developmental biology Histone chemistry Chromatosome biology.protein Biophysics Nucleic Acid Conformation Medicine Protein Multimerization Structural biology Linker 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Scientific Reports, Vol 11, Iss 1, Pp 1-16 (2021) Scientific Reports |
| Popis: | Linker histones play essential roles in the regulation and maintenance of the dynamic chromatin structure of higher eukaryotes. The influence of human histone H1.0 on the nucleosome structure and biophysical properties of the resulting chromatosome were investigated and compared with the 177-bp nucleosome using Cryo-EM and SAXS. The 4.5 Å Cryo-EM chromatosome structure showed that the linker histone binds at the nucleosome dyad interacting with both linker DNA arms but in a tilted manner leaning towards one of the linker sides. The chromatosome is laterally compacted and rigid in the dyad and linker DNA area, in comparison with the nucleosome where linker DNA region is more flexible and displays structural variability. In solution, the chromatosomes appear slightly larger than the nucleosomes, with the volume increase compared to the bound linker histone, according to solution SAXS measurements. SAXS X-ray diffraction characterisation of Mg-precipitated samples showed that the different shapes of the 177 chromatosome enabled the formation of a highly ordered lamello-columnar phase when precipitated by Mg2+, indicating the influence of linker histone on the nucleosome stacking. The biological significance of linker histone, therefore, may be affected by the change in the polyelectrolyte and DNA conformation properties of the chromatosomes, in comparison to nucleosomes. Ministry of Education (MOE) Published version We thank Curt Davey Timothy Richmond for gifts of the plasmids encoding DNA and histones. We appreciate invaluable discussions with Prof Daniela Rhodes. We are indebted to the NTU Institute of Structural Biology (NISB) for the support and use of EM facilities. This work has been supported by the Singapore Ministry of Education Academic Research Fund (AcRF) through a Tier 3 Grant (MOE2012-T3-1-001) and a Tier 1 Grant (2014-T1-001-134). |
| Databáze: | OpenAIRE |
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