2016 Fiscal Year Final Research Report
Molecular mechanism of interaction between transcriptional factors Sp1 and TAF4.
| Project/Area Number |
26440025
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Research Collaborator |
HIBINO Emi 京都大学, 大学院薬学研究科
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Keywords | 転写因子 / 分子間相互作用 / 天然変性蛋白質 / 核磁気共鳴分光法 / グルタミンリッチドメイン |
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| Outline of Final Research Achievements |
The expression of eukaryotic genes is precisely controlled by specific interactions between general transcription initiation factors and gene-specific transcriptional activators. The general transcription factor TFIID plays an essential role in mediating transcriptional activation. On the other hand, biochemical approaches have shown that the promoter-specific transcriptional activator Sp1 interacts with one of the components of TFIID, the TBP-associated factor TAF4.
We herein report the structural details of the glutamine-rich domains (Q-domains) of Sp1 and TAF4. We found that the two Q-domains of Sp1 and four Q-domains of TAF4 were disordered under physiological conditions. We also quantitatively analyzed the interaction between the Q-domains of Sp1 and TAF4 by NMR and surface plasmon resonance, and detected a significant association between them.
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| Free Research Field |
生物物理学
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