Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings

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 nucleoso...

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Detalles Bibliográficos
Autores principales: Sugiyama, Masaaki, Horikoshi, Naoki, Suzuki, Yuya, Taguchi, Hiroyuki, Kujirai, Tomoya, Inoue, Rintaro, Oba, Yojiro, Sato, Nobuhiro, Martel, Anne, Porcar, Lionel, Kurumizaka, Hitoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5668895/
https://www.ncbi.nlm.nih.gov/pubmed/29124184
http://dx.doi.org/10.1016/j.bbrep.2015.08.019
Descripción
Sumario: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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