Crystal Structure of N-Terminal Domain of Tup1 Reveals the Structural Basis for the Assembly of Tup1
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- NAKAMURA Taichi
- Graduate School of Engineering, Osaka University
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- MATSUMURA Hiroyoshi
- Graduate School of Engineering, Osaka University
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- INOUE Tsuyoshi
- Graduate School of Engineering, Osaka University
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- KUSAKA Nanoha
- Nagahama Institute of Bio-Science and Technology
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- TANAKA Naoko
- Nagahama Institute of Bio-Science and Technology
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- MUKAI Yukio
- Nagahama Institute of Bio-Science and Technology
Bibliographic Information
- Other Title
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- 転写制御因子Tup1-N末端ドメインのX線結晶構造とその複合体形成メカニズム
- 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
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Abstract
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.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 55 (2), 110-115, 2013
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679065524736
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- NII Article ID
- 10031168499
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 024694632
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed