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SMC Complexes Are Guarded by the SUMO Protease Ulp2 Against SUMO-Chain-Mediated Turnover
- Publication Year :
- 2020
- Publisher :
- Cold Spring Harbor Laboratory, 2020.
-
Abstract
- Structural maintenance of chromosomes (SMC) 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 ofPDS5null cells and protects cohesin from proteasomal degradation mediated by the SUMO-targeted ubiquitin ligase Slx5/Slx8. The lethality ofPDS5deleted cells can also be bypassed by simultaneous loss of the 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.
- Subjects :
- Saccharomyces cerevisiae Proteins
Chromosomal Proteins, Non-Histone
DNA repair
Condensin
Cell Cycle Proteins
Saccharomyces cerevisiae
macromolecular substances
General Biochemistry, Genetics and Molecular Biology
03 medical and health sciences
0302 clinical medicine
Endopeptidases
Genes, Suppressor
030304 developmental biology
Adenosine Triphosphatases
0303 health sciences
Cohesin
biology
Chemistry
Sumoylation
Chromatin
Cell biology
Proliferating cell nuclear antigen
Ubiquitin ligase
DNA-Binding Proteins
Establishment of sister chromatid cohesion
Protein Subunits
Multiprotein Complexes
Premature chromosome condensation
Mutation
Small Ubiquitin-Related Modifier Proteins
biology.protein
biological phenomena, cell phenomena, and immunity
030217 neurology & neurosurgery
Subjects
Details
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....6c145948a8f7363bb221c534887a120f
- Full Text :
- https://doi.org/10.1101/2020.11.13.381483