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Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4

Author

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  • Yingqi Xu

    (Centre for Structural Biology, Imperial College London)

  • Anna Plechanovová

    (Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee)

  • Peter Simpson

    (Centre for Structural Biology, Imperial College London)

  • Jan Marchant

    (Centre for Structural Biology, Imperial College London)

  • Orsolya Leidecker

    (Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee)

  • Sebastian Kraatz

    (Centre for Structural Biology, Imperial College London)

  • Ronald T. Hay

    (Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee)

  • Steve J. Matthews

    (Centre for Structural Biology, Imperial College London)

Abstract

The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.

Suggested Citation

  • Yingqi Xu & Anna Plechanovová & Peter Simpson & Jan Marchant & Orsolya Leidecker & Sebastian Kraatz & Ronald T. Hay & Steve J. Matthews, 2014. "Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4," Nature Communications, Nature, vol. 5(1), pages 1-12, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5217
    DOI: 10.1038/ncomms5217
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