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Review Article

Twenty years of Mediator complex structural studies

Alexis Verger, Didier Monté, Vincent Villeret
Biochemical Society Transactions Feb 07, 2019, BST20180608; DOI: 10.1042/BST20180608
Alexis Verger
UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France
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  • http://orcid.org/0000-0002-0299-2344
  • For correspondence: alexis.verger@univ-lille.fr
Didier Monté
UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France
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Vincent Villeret
UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, Univ. Lille, F-59000 Lille, France
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Abstract

Mediator is a large multiprotein complex conserved in all eukaryotes that plays an essential role in transcriptional regulation. Mediator comprises 25 subunits in yeast and 30 subunits in humans that form three main modules and a separable four-subunit kinase module. For nearly 20 years, because of its size and complexity, Mediator has posed a formidable challenge to structural biologists. The first two-dimensional electron microscopy (EM) projection map of Mediator leading to the canonical view of its division in three topological modules named Head, Middle and Tail, was published in 1999. Within the last few years, optimization of Mediator purification combined with technical and methodological advances in cryo-electron microscopy (cryo-EM) have revealed unprecedented details of Mediator subunit organization, interactions with RNA polymerase II and parts of its core structure at high resolution. To celebrate the twentieth anniversary of the first Mediator EM reconstruction, we look back on the structural studies of Mediator complex from a historical perspective and discuss them in the light of our current understanding of its role in transcriptional regulation.

  • Cryo-EM
  • Mediator complex
  • structural biology
  • transcription
  • Abbreviations

    ACID/PTOV,
    activator-interacting domain/prostate overexpressed;
    CDK8,
    cyclin-dependent kinase 8;
    cITC,
    core initiation complex;
    CKM,
    CDK8 kinase module;
    cMed,
    core Mediator;
    cryo-EM,
    cryogenic electron microscopy;
    CTD,
    carboxy-terminal domain;
    EM,
    electron microscopy;
    GTF,
    general transcription factor;
    KIX,
    kinase-inducible domain interacting domain;
    MED,
    Mediator;
    PIC,
    PreInitiation complex;
    RNA Pol II,
    RNA polymerase II;
    Srb,
    suppressor of RNA polymerase B;
    TAD,
    transactivation domain
    • © 2019 The Author(s)
    https://creativecommons.org/licenses/by/4.0/

    This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).

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    Twenty years of Mediator complex structural studies
    Alexis Verger, Didier Monté, Vincent Villeret
    Biochemical Society Transactions Feb 2019, BST20180608; DOI: 10.1042/BST20180608
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    Twenty years of Mediator complex structural studies
    Alexis Verger, Didier Monté, Vincent Villeret
    Biochemical Society Transactions Feb 2019, BST20180608; DOI: 10.1042/BST20180608

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      • Abstract
      • Introduction
      • Structural studies of Mediator
      • Structural studies of RNA Pol II–Mediator complexes
      • Conclusion and perspectives
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    Keywords

    cryo-EM
    Mediator complex
    structural biology
    transcription

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