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In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair

Author

Listed:
  • Stefan Peissert

    (University of Würzburg)

  • Florian Sauer

    (University of Würzburg)

  • Daniel B. Grabarczyk

    (University of Würzburg)

  • Cathy Braun

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire Illkirch Cedex, C.U.
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale, U1258
    Université de Strasbourg)

  • Gudrun Sander

    (University of Würzburg)

  • Arnaud Poterszman

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire Illkirch Cedex, C.U.
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale, U1258
    Université de Strasbourg)

  • Jean-Marc Egly

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire Illkirch Cedex, C.U.
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale, U1258
    Université de Strasbourg)

  • Jochen Kuper

    (University of Würzburg)

  • Caroline Kisker

    (University of Würzburg
    Comprehensive Cancer Center Mainfranken)

Abstract

The XPD helicase is a central component of the general transcription factor TFIIH which plays major roles in transcription and nucleotide excision repair (NER). Here we present the high-resolution crystal structure of the Arch domain of XPD with its interaction partner MAT1, a central component of the CDK activating kinase complex. The analysis of the interface led to the identification of amino acid residues that are crucial for the MAT1-XPD interaction. More importantly, mutagenesis of the Arch domain revealed that these residues are essential for the regulation of (i) NER activity by either impairing XPD helicase activity or the interaction of XPD with XPG; (ii) the phosphorylation of the RNA polymerase II and RNA synthesis. Our results reveal how MAT1 shields these functionally important residues thereby providing insights into how XPD is regulated by MAT1 and defining the Arch domain as a major mechanistic player within the XPD scaffold.

Suggested Citation

  • Stefan Peissert & Florian Sauer & Daniel B. Grabarczyk & Cathy Braun & Gudrun Sander & Arnaud Poterszman & Jean-Marc Egly & Jochen Kuper & Caroline Kisker, 2020. "In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15241-9
    DOI: 10.1038/s41467-020-15241-9
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    Cited by:

    1. Hai Wei & Yi M. Weaver & Benjamin P. Weaver, 2024. "Xeroderma pigmentosum protein XPD controls caspase-mediated stress responses," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. R. Čepaitė & N. Klein & A. Mikšys & S. Camara-Wilpert & V. Ragožius & F. Benz & A. Skorupskaitė & H. Becker & G. Žvejytė & N. Steube & G.K.A Hochberg & L. Randau & R. Pinilla-Redondo & L. Malinauskait, 2024. "Structural variation of types IV-A1- and IV-A3-mediated CRISPR interference," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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