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Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs

Author

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  • Nathalia Varejão

    (Universitat Autònoma de Barcelona)

  • Jara Lascorz

    (Universitat Autònoma de Barcelona)

  • Joan Codina-Fabra

    (IRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida)

  • Gemma Bellí

    (IRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida)

  • Helena Borràs-Gas

    (Universitat Autònoma de Barcelona)

  • Jordi Torres-Rosell

    (IRBLLEIDA, Dept. Ciències Mèdiques Bàsiques, Universitat de Lleida)

  • David Reverter

    (Universitat Autònoma de Barcelona)

Abstract

Post-translational modification of proteins by ubiquitin and ubiquitin-like modifiers, such as SUMO, are key events in protein homeostasis or DNA damage response. Smc5/6 is a nuclear multi-subunit complex that participates in the recombinational DNA repair processes and is required in the maintenance of chromosome integrity. Nse2 is a subunit of the Smc5/6 complex that possesses SUMO E3 ligase activity by the presence of a SP-RING domain that activates the E2~SUMO thioester for discharge on the substrate. Here we present the crystal structure of the SUMO E3 ligase Nse2 in complex with an E2-SUMO thioester mimetic. In addition to the interface between the SP-RING domain and the E2, the complex reveals how two SIM (SUMO-Interacting Motif) -like motifs in Nse2 are restructured upon binding the donor and E2-backside SUMO during the E3-dependent discharge reaction. Both SIM interfaces are essential in the activity of Nse2 and are required to cope with DNA damage.

Suggested Citation

  • Nathalia Varejão & Jara Lascorz & Joan Codina-Fabra & Gemma Bellí & Helena Borràs-Gas & Jordi Torres-Rosell & David Reverter, 2021. "Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27301-9
    DOI: 10.1038/s41467-021-27301-9
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    References listed on IDEAS

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    1. David Reverter & Christopher D. Lima, 2005. "Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex," Nature, Nature, vol. 435(7042), pages 687-692, June.
    2. Anna Plechanovová & Ellis G. Jaffray & Michael H. Tatham & James H. Naismith & Ronald T. Hay, 2012. "Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis," Nature, Nature, vol. 489(7414), pages 115-120, September.
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