ArticlePLoS biology2015
ATPase-dependent control of the Mms21 SUMO ligase during DNA repair.
Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- The Multifunctional SMC5/6 Complex in Genome Stability, Antiviral Restriction, and Human Disease.Current issues in molecular biology · 2026Review
- Multi-subunit collaboration enables Smc5/6 to function as a composite SUMO E3 complex.Nature communications · 2026Article
- Ligase-dependent and independent functions of the C-terminus of Mms21 contribute to optimal growth and genome stability inMolecular biology of the cell · 2026Article
- Structural and mechanistic perspectives on Nse5/6 regulation of the Smc5/6 complex.Frontiers in molecular biosciences · 2026Review
- 4G cloning: rapid gene assembly for expression of multisubunit protein complexes in diverse hosts.Life science alliance · 2025Article
- In Vitro SUMOylation Assays with a DNA-Sensitive Multi-subunit E3 Ligase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Human Smc5/6 recognises transcription-generated positive DNA supercoils.Nature communications · 2024Article
- Crucial role of the NSE1 RING domain in Smc5/6 stability and FANCM-independent fork progression.Cellular and molecular life sciences : CMLS · 2024Article
- The SMC5/6 complex: folding chromosomes back into shape when genomes take a break.Nucleic acids research · 2024Review
- The multi-functional Smc5/6 complex in genome protection and disease.Nature structural & molecular biology · 2023Review
- Smc5/6 silences episomal transcription by a three-step function.Nature structural & molecular biology · 2022Article
- Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.Nature communications · 2021Article
- Acute ethanol stress induces sumoylation of conserved chromatin structural proteins inMolecular biology of the cell · 2021Article
- Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction.Molecular cell · 2020Article
- A natural variant of the essential host geneeLife · 2020Article
- Review
- Recruitment, loading, and activation of the Smc5-Smc6 SUMO ligase.Current genetics · 2019Review
- DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex.The EMBO journal · 2018Article
- SUMOylome Profiling Reveals a Diverse Array of Nuclear Targets Modified by the SUMO Ligase SIZ1 during Heat Stress.The Plant cell · 2018Article
- Smc5/6 complex regulates Sgs1 recombination functions.Current genetics · 2017Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modification of proteins by SUMO is essential for the maintenance of genome integrity. During DNA replication, the Mms21-branch of the SUMO pathway counteracts recombination intermediates at damaged replication forks, thus facilitating sister chromatid disjunction. The Mms21 SUMO ligase docks to the arm region of the Smc5 protein in the Smc5/6 complex; together, they cooperate during recombinational DNA repair. Yet how the activity of the SUMO ligase is controlled remains unknown. Here we show that the SUMO ligase and the chromosome disjunction functions of Mms21 depend on its docking to an intact and active Smc5/6 complex, indicating that the Smc5/6-Mms21 complex operates as a large SUMO ligase in vivo. In spite of the physical distance separating the E3 and the nucleotide-binding domains in Smc5/6, Mms21-dependent sumoylation requires binding of ATP to Smc5, a step that is part of the ligase mechanism that assists Ubc9 function. The communication is enabled by the presence of a conserved disruption in the coiled coil domain of Smc5, pointing to potential conformational changes for SUMO ligase activation. In accordance, scanning force microscopy of the Smc5-Mms21 heterodimer shows that the molecule is physically remodeled in an ATP-dependent manner. Our results demonstrate that the ATP-binding activity of the Smc5/6 complex is coordinated with its SUMO ligase, through the coiled coil domain of Smc5 and the physical remodeling of the molecule, to promote sumoylation and chromosome disjunction during DNA repair.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.