ArticleBMC biochemistry2011
SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.
Article in BMC biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- DeSUMOylation of Spastin Enhances AMPA Receptor Recycling and Synaptic Plasticity via IST1-Dependent Endosomal Sorting.Molecular neurobiology · 2025Article
- The TDG protein environment connects active DNA demethylation with chromatin and RNA biology.Cellular and molecular life sciences : CMLS · 2025Article
- Protein-Protein Interactions in Base Excision Repair.Biomolecules · 2025Review
- Post-translational modifications in DNA damage repair: mechanisms underlying temozolomide resistance in glioblastoma.Oncogene · 2025Review
- Potential role of PIM1 inhibition in the treatment of SARS-CoV-2 infection.Journal, genetic engineering & biotechnology · 2023Article
- Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.Structure (London, England : 1993) · 2020Article
- Desumoylation of RNA polymerase III lies at the core of the Sumo stress response in yeast.The Journal of biological chemistry · 2019Article
- Identification of a noncanonical RNA binding domain in the U2 snRNP protein SF3A1.RNA (New York, N.Y.) · 2019Article
- SUMOylation coordinates BERosome assembly in active DNA demethylation during cell differentiation.The EMBO journal · 2019Article
- Defining the impact of sumoylation on substrate binding and catalysis by thymine DNA glycosylase.Nucleic acids research · 2018Article
- SUMO, a small, but powerful, regulator of double-strand break repair.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Regulation of DNA demethylation by the XPC DNA repair complex in somatic and pluripotent stem cells.Genes & development · 2017Article
- Identification of SUMO modification sites in the base excision repair protein, Ntg1.DNA repair · 2016Article
- Base Excision Repair, a Pathway Regulated by Posttranslational Modifications.Molecular and cellular biology · 2016Review
- Characterizing Requirements for Small Ubiquitin-like Modifier (SUMO) Modification and Binding on Base Excision Repair Activity of Thymine-DNA Glycosylase in Vivo.The Journal of biological chemistry · 2016Article
- The current state of eukaryotic DNA base damage and repair.Nucleic acids research · 2015Review
- SUMO-mediated regulation of DNA damage repair and responses.Trends in biochemical sciences · 2015Review
- A germline polymorphism of thymine DNA glycosylase induces genomic instability and cellular transformation.PLoS genetics · 2014Article
- Thymine DNA glycosylase is a CRL4Cdt2 substrate.The Journal of biological chemistry · 2014Article
- E2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex.The Journal of biological chemistry · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe human thymine-DNA glycosylase (TDG) plays a dual role in base excision repair of G:U/T mismatches and in transcription. Regulation of TDG activity by SUMO-1 conjugation was shown to act on both functions. Furthermore, TDG can interact with SUMO-1 in a non-covalent manner.
resultsUsing NMR spectroscopy we have determined distinct conformational changes in TDG upon either covalent sumoylation on lysine 330 or intermolecular SUMO-1 binding through a unique SUMO-binding motif (SBM) localized in the C-terminal region of TDG. The non-covalent SUMO-1 binding induces a conformational change of the TDG amino-terminal regulatory domain (RD). Such conformational dynamics do not exist with covalent SUMO-1 attachment and could potentially play a broader role in the regulation of TDG functions for instance during transcription. Both covalent and non-covalent processes activate TDG G:U repair similarly. Surprisingly, despite a dissociation of the SBM/SUMO-1 complex in presence of a DNA substrate, SUMO-1 preserves its ability to stimulate TDG activity indicating that the non-covalent interactions are not directly involved in the regulation of TDG activity. SUMO-1 instead acts, as demonstrated here, indirectly by competing with the regulatory domain of TDG for DNA binding.
conclusionsSUMO-1 increases the enzymatic turnover of TDG by overcoming the product-inhibition of TDG on apurinic sites. The mechanism involves a competitive DNA binding activity of SUMO-1 towards the regulatory domain of TDG. This mechanism might be a general feature of SUMO-1 regulation of other DNA-bound factors such as transcription regulatory proteins.
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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.