論文

査読有り
2017年11月

Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution nuclear magnetic resonance spectroscopy

PROTEIN SCIENCE
  • Emi Hibino
  • ,
  • Rintaro Inoue
  • ,
  • Masaaki Sugiyama
  • ,
  • Jun Kuwahara
  • ,
  • Katsumi Matsuzaki
  • ,
  • Masaru Hoshino

26
11
開始ページ
2280
終了ページ
2290
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/pro.3287
出版者・発行元
WILEY

The expression of eukaryotic genes is precisely controlled by interactions between general transcriptional factors and promoter-specific transcriptional activators. The fourth element of TATA-box binding protein-associated factor (TAF4), an essential subunit of the general transcription factor TFIID, serves as a coactivator for various promoter-specific transcriptional regulators. Interactions between TAF4 and site-specific transcriptional activators, such as Sp1, are important for regulating the expression levels of genes of interest. However, only limited information is available on the molecular mechanisms underlying the interactions between these transcriptional regulatory proteins. We herein analyzed the interaction between the transcriptional factors Sp1 and TAF4 using high-resolution solution nuclear magnetic resonance spectroscopy. We found that four glutamine-rich (Q-rich) regions in TAF4 were largely disordered under nearly physiological conditions. Among them, the first Q-rich region in TAF4 was essential for the interaction with another Q-rich region in the Sp1 molecule, most of which was largely disordered. The residues responsible for this interaction were specific and highly localized in a defined region within a range of 20-30 residues. Nevertheless, a detailed analysis of C-13-chemical shift values suggested that no significant conformational change occurred upon binding. These results indicate a prominent and exceptional binding mode for intrinsically disordered proteins other than the well-accepted concept of coupled folding and binding."

Web of Science ® 被引用回数 : 3

リンク情報
DOI
https://doi.org/10.1002/pro.3287
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/28857320
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000413668900016&DestApp=WOS_CPL