2015年12月1日
Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings
Biochemistry and Biophysics Reports
- 巻
- 4
- 号
- 開始ページ
- 28
- 終了ページ
- 32
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrep.2015.08.019
- 出版者・発行元
- Elsevier
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.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.bbrep.2015.08.019
- ISSN : 2405-5808
- PubMed ID : 29124184
- SCOPUS ID : 84940658170