NMR structure of the human Mediator MED25 ACID domain. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Structural Biology Année : 2011

NMR structure of the human Mediator MED25 ACID domain.

Alexis Verger
Frédérique Dewitte
  • Fonction : Auteur
Zoé Lens
  • Fonction : Auteur
Jean-Luc Baert
  • Fonction : Auteur
Elisabeth Ferreira
  • Fonction : Auteur
Yvan de Launoit
  • Fonction : Auteur
Vincent Villeret
  • Fonction : Auteur
Didier Monté

Résumé

MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed β-barrel with seven strands (Β1-Β7) and three α-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the β-barrel, defined by strands B4-B7-B6.

Domaines

Chimie organique

Dates et versions

hal-00589014 , version 1 (27-04-2011)

Identifiants

Citer

François Bontems, Alexis Verger, Frédérique Dewitte, Zoé Lens, Jean-Luc Baert, et al.. NMR structure of the human Mediator MED25 ACID domain.. Journal of Structural Biology, 2011, 174 (1), pp.245-51. ⟨10.1016/j.jsb.2010.10.011⟩. ⟨hal-00589014⟩
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