ArticleProceedings of the National Academy of Sciences of the United States of America2012
Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 84 citations in OpenAlex.
- Structural basis of cyclobutane pyrimidine dimer recognition by UV-DDB in the nucleosome.Nature communications · 2025Article
- XPC-RAD23B enhances UV-DDB binding to DNA to facilitate lesion search in nucleotide excision repair.Nucleic acids research · 2025Article
- A Target Class Ligandability Evaluation of WD40 Repeat-Containing Proteins.Journal of medicinal chemistry · 2025Article
- Disrupting DDB2-DNA Interaction by Lapatinib Enhances Chemotherapy Sensitivity.International journal of biological sciences · 2025Article
- Detection of oxaliplatin- and cisplatin-DNA lesions requires different global genome repair mechanisms that affect their clinical efficacy.NAR cancer · 2023Article
- Symmetric control of sister chromatid cohesion establishment.Nucleic acids research · 2023Article
- Dynamic conformational switching underlies TFIIH function in transcription and DNA repair and impacts genetic diseases.Nature communications · 2023Article
- UV irradiation remodels the specificity landscape of transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- Structural modeling and analyses of genetic variations in the human XPC nucleotide excision repair protein.Journal of biomolecular structure & dynamics · 2023Article
- Proteomic Analysis of Nuclear Hepatitis B Virus Relaxed Circular DNA-Associated Proteins Identifies UV-Damaged DNA Binding Protein as a Host Factor Involved in Covalently Closed Circular DNA Formation.Journal of virology · 2022Article
- Impact of DNA sequences on DNA 'opening' by the Rad4/XPC nucleotide excision repair complex.DNA repair · 2021Article
- Single molecule analysis indicates stimulation of MUTYH by UV-DDB through enzyme turnover.Nucleic acids research · 2021Article
- 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
- UbiNet 2.0: a verified, classified, annotated and updated database of E3 ubiquitin ligase-substrate interactions.Database : the journal of biological databases and curation · 2021Article
- A novel DDB2 mutation causes defective recognition of UV-induced DNA damages and prevalent equine squamous cell carcinoma.DNA repair · 2021Article
- Searching for DNA Damage: Insights From Single Molecule Analysis.Frontiers in molecular biosciences · 2021Review
- The involvement of nucleotide excision repair proteins in the removal of oxidative DNA damage.Nucleic acids research · 2020Review
- Review
- Losses of human disease-associated genes in placental mammals.NAR genomics and bioinformatics · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
UV light-induced photoproducts are recognized and removed by the nucleotide-excision repair (NER) pathway. In humans, the UV-damaged DNA-binding protein (UV-DDB) is part of a ubiquitin E3 ligase complex (DDB1-CUL4A(DDB2)) that initiates NER by recognizing damaged chromatin with concomitant ubiquitination of core histones at the lesion. We report the X-ray crystal structure of the human UV-DDB in a complex with damaged DNA and show that the N-terminal domain of DDB2 makes critical contacts with two molecules of DNA, driving N-terminal-domain folding and promoting UV-DDB dimerization. The functional significance of the dimeric UV-DDB [(DDB1-DDB2)(2)], in a complex with damaged DNA, is validated by electron microscopy, atomic force microscopy, solution biophysical, and functional analyses. We propose that the binding of UV-damaged DNA results in conformational changes in the N-terminal domain of DDB2, inducing helical folding in the context of the bound DNA and inducing dimerization as a function of nucleotide binding. The temporal and spatial interplay between domain ordering and dimerization provides an elegant molecular rationale for the unprecedented binding affinities and selectivities exhibited by UV-DDB for UV-damaged DNA. Modeling the DDB1-CUL4A(DDB2) complex according to the dimeric UV-DDB-AP24 architecture results in a mechanistically consistent alignment of the E3 ligase bound to a nucleosome harboring damaged DNA. Our findings provide unique structural and conformational insights into the molecular architecture of the DDB1-CUL4A(DDB2) E3 ligase, with significant implications for the regulation and overall organization of the proteins responsible for initiation of NER in the context of chromatin and for the consequent maintenance of genomic integrity.
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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.