ArticleDNA repair2011
A role for SUMO in nucleotide excision repair.
Article in DNA repair, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Sequential post-translational modifications regulate damaged DNA-binding protein DDB2 function.Journal of biochemistry · 2024Article
- Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair.Nucleic acids research · 2024Article
- Chaperones for dancing on chromatin: Role of post-translational modifications in dynamic damage detection hand-offs during nucleotide excision repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Article
- Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020Review
- A SUMO-dependent pathway controls elongating RNA Polymerase II upon UV-induced damage.Scientific reports · 2019Article
- The Nup84 complex coordinates the DNA damage response to warrant genome integrity.Nucleic acids research · 2019Article
- SUMOylation in Glioblastoma: A Novel Therapeutic Target.International journal of molecular sciences · 2019Review
- Global Identification of Small Ubiquitin-related Modifier (SUMO) Substrates Reveals Crosstalk between SUMOylation and Phosphorylation Promotes Cell Migration.Molecular & cellular proteomics : MCP · 2018Article
- Identification of SUMO conjugation sites in the budding yeast proteome.Microbial cell (Graz, Austria) · 2017Article
- Genome maintenance in Saccharomyces cerevisiae: the role of SUMO and SUMO-targeted ubiquitin ligases.Nucleic acids research · 2017Review
- A comprehensive compilation of SUMO proteomics.Nature reviews. Molecular cell biology · 2016Article
- Smc5/6 Mediated Sumoylation of the Sgs1-Top3-Rmi1 Complex Promotes Removal of Recombination Intermediates.Cell reports · 2016Article
- Implication of SUMO E3 ligases in nucleotide excision repair.Cytotechnology · 2015Article
- SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair.Nature communications · 2015Article
- SUMO-mediated regulation of DNA damage repair and responses.Trends in biochemical sciences · 2015Review
- Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway.The Journal of biological chemistry · 2015Article
- SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage.Cell reports · 2015Article
- NRMT1 knockout mice exhibit phenotypes associated with impaired DNA repair and premature aging.Mechanisms of ageing and development · 2015Article
- Sumoylation influences DNA break repair partly by increasing the solubility of a conserved end resection protein.PLoS genetics · 2015Article
- Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The two Siz/PIAS SUMO E3 ligases Siz1 and Siz2 are responsible for the vast majority of sumoylation in Saccharomyces cerevisiae. We found that siz1Δ siz2Δ mutants are sensitive to ultra-violet (UV) light. Epistasis analysis showed that the SIZ genes act in the nucleotide excision repair (NER) pathway, and suggested that they participate both in global genome repair (GGR) and in the Rpb9-dependent subpathway of transcription-coupled repair (TCR), but have minimal role in Rad26-dependent TCR. Quantitative analysis of NER at the single-nucleotide level showed that siz1Δ siz2Δ is deficient in repair of both the transcribed and non-transcribed strands of the DNA. These experiments confirmed that the SIZ genes participate in GGR. Their role in TCR remains unclear. It has been reported previously that mutants deficient for the SUMO conjugating enzyme Ubc9 contain reduced levels of Rad4, the yeast homolog of human XPC. However, our experiments do not support the conclusion that SUMO conjugation affects Rad4 levels. We found that several factors that participate in NER are sumoylated, including Rad4, Rad16, Rad7, Rad1, Rad10, Ssl2, Rad3, and Rpb4. Although Rad16 was heavily sumoylated, elimination of the major SUMO attachment sites in Rad16 had no detectable effect on UV resistance or removal of DNA lesions. SUMO attachment to most of these NER factors was significantly increased by DNA damage. Furthermore, SUMO-modified Rad4 accumulated in NER mutants that block the pathway downstream of Rad4, suggesting that SUMO becomes attached to Rad4 at a specific point during its functional cycle. Collectively, these results suggest that SIZ-dependent sumoylation may modulate the activity of multiple proteins to promote efficient NER.
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Registered trials
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.