Structural basis for the interaction between p53 transactivation domain and the mediator subunit MED25

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Title
Structural basis for the interaction between p53 transactivation domain and the mediator subunit MED25
Author(s)
Min-Sung Lee; Kyungeun Lim; Mi-Kyung LeeSeung-Wook Chi
Bibliographic Citation
Molecules, vol. 23, no. 10, pp. e2726-e2726
Publication Year
2018
Abstract
Eukaryotic transcription initiation is mediated by interactions between transcriptional activators and the mediator coactivator complex. Molecular interaction of p53 transcription factor with mediator complex subunit 25 (MED25) is essential for its target gene transcription. In this study, we characterized the molecular interaction between p53 transactivation domain (p53TAD) and activator interaction domain (ACID) of MED25 using nuclear magnetic resonance (NMR) spectroscopy. The NMR chemical shift perturbation and isothermal titration calorimetry (ITC) data showed that p53TAD interacted with MED25 ACID mainly through the p53TAD2 sequence motif. Taken together with the mutagenesis data, the refined structural model of MED25 ACID/p53TAD2 peptide complex showed that an amphipathic α-helix of p53TAD2 peptide bound an elongated hydrophobic groove of MED25 ACID. Furthermore, our results revealed the highly conserved mechanism of MED25 interaction with intrinsically unfolded acidic TADs from the transcriptional activators p53, ERM (Ets-related molecule), and herpes simplex virus protein 16 (VP16).
Keyword
MED25complex structurenuclear magnetic resonancep53protein-protein interactiontransactivation domain
ISSN
1420-3049
Publisher
MDPI
DOI
http://dx.doi.org/10.3390/molecules23102726
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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