Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.
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.
Mesh Terms:
Basic Helix-Loop-Helix Transcription Factors, Biomimetics, Cell Cycle Proteins, Crystallography, X-Ray, DNA Damage, Protein Processing, Post-Translational, Proteostasis, Recombinational DNA Repair, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Ubiquitin-Related Modifier Proteins, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
Basic Helix-Loop-Helix Transcription Factors, Biomimetics, Cell Cycle Proteins, Crystallography, X-Ray, DNA Damage, Protein Processing, Post-Translational, Proteostasis, Recombinational DNA Repair, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Ubiquitin-Related Modifier Proteins, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
Nat Commun
Date: Dec. 01, 2020
PubMed ID: 34853311
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