SMC complexes are guarded by the SUMO protease Ulp2 against SUMO-chain-mediated turnover.
Structural maintenance of chromosomes (SMCs) complexes, cohesin, condensin, and Smc5/6, are essential for viability and participate in multiple processes, including sister chromatid cohesion, chromosome condensation, and DNA repair. Here we show that SUMO chains target all three SMC complexes and are antagonized by the SUMO protease Ulp2 to prevent their turnover. ... We uncover that the essential role of the cohesin-associated subunit Pds5 is to counteract SUMO chains jointly with Ulp2. Importantly, fusion of Ulp2 to kleisin Scc1 supports viability of PDS5 null cells and protects cohesin from proteasomal degradation mediated by the SUMO-targeted ubiquitin ligase Slx5/Slx8. The lethality of PDS5-deleted cells can also be bypassed by simultaneous loss of the proliferating cell nuclear antigen (PCNA) unloader, Elg1, and the cohesin releaser, Wpl1, but only when Ulp2 is functional. Condensin and Smc5/6 complex are similarly guarded by Ulp2 against unscheduled SUMO chain assembly, which we propose to time the availability of SMC complexes on chromatin.
Mesh Terms:
Adenosine Triphosphatases, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Endopeptidases, Genes, Suppressor, Multiprotein Complexes, Mutation, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Ubiquitin-Related Modifier Proteins, Sumoylation
Adenosine Triphosphatases, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Endopeptidases, Genes, Suppressor, Multiprotein Complexes, Mutation, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Ubiquitin-Related Modifier Proteins, Sumoylation
Cell Rep
Date: Aug. 03, 2021
PubMed ID: 34348159
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