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Title 

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

Authors 

Min-Sung LeeKyungeun LimMi-Kyung LeeSeung-Wook Chi

Publisher 

MDPI

Issue Date 

2018

Citation 

Molecules

Keywords 

MED25complex structurenuclear magnetic resonancep53protein-protein interactiontransactivation domain

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).

ISSN 

1420-3049

Link 

http://dx.doi.org/10.3390/molecules23102726

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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