Removal of histone tails from nucleosome dissects the physical mechanisms of salt-induced aggregation, linker histone H1-induced compaction, and 30-nm fiber formation of the nucleosome array

• 日詰, 光治

• 竹安, 邦夫

• Araki, Sumiko

• Prieto, Eloise

• Yoshikawa, Kenichi

• Takeyasu, Kunio

抄録

In order to reveal the roles of histone tails in the formation of higher-order chromatin structures, we employed atomic force microscopy (AFM), and an in vitro reconstitution system to examine the properties of reconstituted chromatin composed of tail-less histones and a long DNA (106-kb plasmid) template. The tail-less nucleosomes did not aggregate at high salt concentrations or with an excess amount of core histones, in contrast with the behavior of nucleosomal arrays composed of nucleosomes containing normal, N-terminal tails. Analysis of our nucleosome distributions reveals that the attractive interaction between tail-less nucleosomes is weakened. Addition of linker histone H1 into the tail-less nucleosomal array failed to promote the formation of 30 nm chromatin fibers that are usually formed in the normal nucleosomal array. These results demonstrate that the attractive interaction between nucleosomes via histone tails plays a critical role in the formation of the uniform 30-nm chromatin fiber.

収録刊行物

• Ultramicroscopy

  Ultramicroscopy 109 (8), 868-873, 2009-07

  Elsevier

キーワード

• Atomic force microscopy
• Chromatin
• Electron microscopy
• Histone tail
• Nucleosome
• Scanning tunneling and atomic force microscopy

詳細情報

• CRID: 1050282677039802112
• NII論文ID: 120001468043
• ISSN: 03043991
• HANDLE: 2433/84728
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles