Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4
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- Emi Hibino
- Graduate School of Pharmaceutical Sciences Kyoto University 46‐29 Yoshida‐Shimoadachi Sakyo‐Ku Kyoto 606‐8501 Japan
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- Rintaro Inoue
- Research Reactor Institute, Kyoto University Kumatori Sennan‐Gun Osaka 590‐0494 Japan
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- Masaaki Sugiyama
- Research Reactor Institute, Kyoto University Kumatori Sennan‐Gun Osaka 590‐0494 Japan
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- Jun Kuwahara
- Faculty of Pharmaceutical Sciences Doshisha Women's University Kodo Kyotanabe City 610‐0395 Japan
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- Katsumi Matsuzaki
- Graduate School of Pharmaceutical Sciences Kyoto University 46‐29 Yoshida‐Shimoadachi Sakyo‐Ku Kyoto 606‐8501 Japan
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- Masaru Hoshino
- Graduate School of Pharmaceutical Sciences Kyoto University 46‐29 Yoshida‐Shimoadachi Sakyo‐Ku Kyoto 606‐8501 Japan
Abstract
<jats:title>Abstract</jats:title><jats:p>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, which plays an essential role in mediating transcriptional activation, is a multisubunit complex comprising the TATA box‐binding protein (TBP) and multiple TBP‐associated factors (TAFs). On the other hand, biochemical and genetic approaches have shown that the promoter‐specific transcriptional activator Sp1 has the ability to interact 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 using circular dichroism (CD) and heteronuclear magnetic resonance (NMR) spectroscopy. 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 weak but specific association between them. Nevertheless, a detailed analysis of CD spectra suggested that any significant conformational change did not occur concomitantly with this association, at least at the level of the overall secondary structure. These results may represent a prominent and exceptional binding mode for the IDPs, which are not categorized in a well‐accepted concept of “coupled folding and binding.”</jats:p>
Journal
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- Protein Science
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Protein Science 25 (11), 2006-2017, 2016-08-24
Wiley
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Details 詳細情報について
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- CRID
- 1360848655200751744
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- DOI
- 10.1002/pro.3013
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- ISSN
- 1469896X
- 09618368
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- Data Source
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- Crossref
- KAKEN