ArticleNucleic acids research2005
T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- Multifaceted nucleic acid probing with a rationally upgraded molecular rotor.Chemical science · 2024Article
- Kinetic Analysis of the Effect ofBiochemistry · 2022Article
- The Role of Thymine DNA Glycosylase in Transcription, Active DNA Demethylation, and Cancer.Cancers · 2022Review
- Nucleosomes and the three glycosylases: High, medium, and low levels of excision by the uracil DNA glycosylase superfamily.DNA repair · 2018Article
- BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.DNA repair · 2017Review
- Oestrogen receptor β regulates epigenetic patterns at specific genomic loci through interaction with thymine DNA glycosylase.Epigenetics & chromatin · 2016Article
- Multifaceted roles for thymine DNA glycosylase in embryonic development and human carcinogenesis.Acta biochimica et biophysica Sinica · 2016Review
- The current state of eukaryotic DNA base damage and repair.Nucleic acids research · 2015Review
- APOBEC3B-Mediated Cytidine Deamination Is Required for Estrogen Receptor Action in Breast Cancer.Cell reports · 2015Article
- 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
- Co-regulated gene expression by oestrogen receptor α and liver receptor homolog-1 is a feature of the oestrogen response in breast cancer cells.Nucleic acids research · 2013Article
- DNA demethylation by TDG.Epigenomics · 2012Review
- Identification of novel interacting partners of Sirtuin6.PloS one · 2012Article
- Active DNA demethylation in plants and animals.Cold Spring Harbor symposia on quantitative biology · 2012Review
- SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.BMC biochemistry · 2011Article
- Immortal coils: conserved dimerization motifs of the Drosophila ovulation prohormone ovulin.Insect biochemistry and molecular biology · 2010Article
- Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase.Nucleic acids research · 2010Article
- The interaction between thymine DNA glycosylase and nuclear receptor coactivator 3 is required for the transcriptional activation of nuclear hormone receptors.Molecular and cellular biochemistry · 2010Article
- Thymine DNA glycosylase represses myocardin-induced smooth muscle cell differentiation by competing with serum response factor for myocardin binding.The Journal of biological chemistry · 2008Article
- Serial ChIP as a tool to investigate the co-localization or exclusion of proteins on plant genes.Plant methods · 2008Article
Corrections and comments
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Authors and funding
16 authors at 1 institution in 1 country.
Funding
Abstract
Gene activation involves protein complexes with diverse enzymatic activities, some of which are involved in chromatin modification. We have shown previously that the base excision repair enzyme thymine DNA glycosylase (TDG) acts as a potent coactivator for estrogen receptor-alpha. To further understand how TDG acts in this context, we studied its interaction with known coactivators of nuclear receptors. We find that TDG interacts in vitro and in vivo with the p160 coactivator SRC1, with the interaction being mediated by a previously undescribed motif encoding four equally spaced tyrosine residues in TDG, each tyrosine being separated by three amino acids. This is found to interact with two motifs in SRC1 also containing tyrosine residues separated by three amino acids. Site-directed mutagenesis shows that the tyrosines encoded in these motifs are critical for the interaction. The related p160 protein TIF2 does not interact with TDG and has the altered sequence, F-X-X-X-Y, at the equivalent positions relative to SRC1. Substitution of the phenylalanines to tyrosines is sufficient to bring about interaction of TIF2 with TDG. These findings highlight a new protein-protein interaction motif based on Y-X-X-X-Y and provide new insight into the interaction of diverse proteins in coactivator complexes.
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