Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings |
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Authors: | Masaaki Sugiyama Naoki Horikoshi Yuya Suzuki Hiroyuki Taguchi Tomoya Kujirai Rintaro Inoue Yojiro Oba Nobuhiro Sato Anne Martel Lionel Porcar Hitoshi Kurumizaka |
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Affiliation: | 1. Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan;2. Laboratory of Structural Biology, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan;3. Research Institute for Science and Engineering, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan;4. Institut Laue-Langevin, 6, rue Jules Horowitz, Grenoble 38042, France |
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Abstract: | Solution structures of nucleosomes containing a human histone variant, H2A.Z.1, were measured by small-angle X-ray and neutron scatterings (SAXS and SANS). SAXS revealed that the outer shape, reflecting the DNA shape, of the H2A.Z.1 nucleosome is almost the same as that of the canonical H2A nucleosome. In contrast, SANS employing a contrast variation technique revealed that the histone octamer of the H2A.Z.1 nucleosome is smaller than that of the canonical nucleosome. The DNA within the H2A.Z.1 nucleosome was more susceptible to micrococcal nuclease than that within the canonical nucleosome. These results suggested that the DNA is loosely wrapped around the histone core in the H2A.Z.1 nucleosome. |
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Keywords: | Nucleosome H2A.Z.1 Small-angle X-ray scattering Small-angle neutron scattering Contrast variation Stuhrmann plot |
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