We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Structural Basis for the Interaction between p53 Transactivation Domain and the Mediator Subunit MED25.
- Authors
Lee, Min-Sung; Lim, Kyungeun; Lee, Mi-Kyung; Chi, Seung-Wook
- 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).
- Subjects
MOLECULAR interactions; TRANSCRIPTION factors; GENETIC transcription; NUCLEAR magnetic resonance; HYDROPHOBIC interactions; HERPES simplex virus
- Publication
Molecules, 2018, Vol 23, Issue 10, p2726
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules23102726