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

Nathalia Varejão, Jara Lascorz, Joan Codina-Fabra, Gemma Bellí, Helena Borràs-Gas, Jordi Torres-Rosell and David Reverter ()
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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

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-27301-9

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