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- 中村 太一
- Graduate School of Engineering, Osaka University
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- 松村 浩由
- Graduate School of Engineering, Osaka University
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- 井上 豪
- Graduate School of Engineering, Osaka University
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- 日下 菜花
- Nagahama Institute of Bio-Science and Technology
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- 田中 直子
- Nagahama Institute of Bio-Science and Technology
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- 向 由起夫
- Nagahama Institute of Bio-Science and Technology
書誌事項
- タイトル別名
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- Crystal Structure of N-Terminal Domain of Tup1 Reveals the Structural Basis for the Assembly of Tup1
- テンシャ セイギョ インシ Tup1-N マッタン ドメイン ノ Xセン ケッショウ コウゾウ ト ソノ フクゴウタイ ケイセイ メカニズム
この論文をさがす
抄録
The Tup1-Cyc8 complex acts as a corepressor for members of multiple families of transcription factors. Although its physiological functions have been extensively studied, it remained unclear how the corepressor assembles, and how the assembly involves in the molecular functions. Here, we report the crystal structure of N-terminal domain of Tup1, which is essential for its self-assembly and interaction with Cyc8. The N-terminal domain of Tup1 tetramerizes to form a novel antiparallel four-helix bundle, and is organized as a dimer of dimers. Coiled-coil interactions stabilize each dimer together, and mutagenesis study confirmed that the hydrophobic residues responsible for the association of the protomers as dimers are required for transcriptional repression. We confirmed the functional and structural importance of the hydrophobic residues by further X-ray crystallography.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 55 (2), 110-115, 2013
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390282679065524736
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- NII論文ID
- 10031168499
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 024694632
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可