ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Rad1-Rad10 uses different interfaces to interact with pathway-specific DNA repair factors.Nucleic acids research · 2026Article
- Generation of site-specifically labelled fluorescent human XPA to investigate DNA binding dynamics during nucleotide excision repair.Methods (San Diego, Calif.) · 2024Article
- Article
- The XPA Protein-Life under Precise Control.Cells · 2022Review
- Impact of DNA sequences on DNA 'opening' by the Rad4/XPC nucleotide excision repair complex.DNA repair · 2021Article
- Tethering-facilitated DNA 'opening' and complementary roles of β-hairpin motifs in the Rad4/XPC DNA damage sensor protein.Nucleic acids research · 2020Article
- Envisioning how the prototypic molecular machine TFIIH functions in transcription initiation and DNA repair.DNA repair · 2020Review
- Single molecule analysis reveals monomeric XPA bends DNA and undergoes episodic linear diffusion during damage search.Nature communications · 2020Article
- A key interaction with RPA orients XPA in NER complexes.Nucleic acids research · 2020Article
- Structural basis of TFIIH activation for nucleotide excision repair.Nature communications · 2019Article
- The redefined DNA-binding domain of human xeroderma pigmentosum complementation group A: production, crystallization and structure solution.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Tdp1 processes chromate-induced single-strand DNA breaks that collapse replication forks.PLoS genetics · 2018Article
- Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates.The Journal of biological chemistry · 2017Article
- Design and Structure-Guided Development of Novel Inhibitors of the Xeroderma Pigmentosum Group A (XPA) Protein-DNA Interaction.Journal of medicinal chemistry · 2017Article
- Chromatin Regulates Genome Targeting with Cisplatin.Angewandte Chemie (International ed. in English) · 2017Article
- Both DNA global deformation and repair enzyme contacts mediate flipping of thymine dimer damage.Scientific reports · 2017Article
- Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.The Journal of biological chemistry · 2016Article
- XPA: A key scaffold for human nucleotide excision repair.DNA repair · 2016Review
- Metal binding mediated conformational change of XPA protein:a potential cytotoxic mechanism of nickel in the nucleotide excision repair.Journal of molecular modeling · 2016Article
- Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assembly.Computational and structural biotechnology journal · 2016Review
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10 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Nucleotide excision repair (NER) is responsible for the removal of a large variety of structurally diverse DNA lesions. Mutations of the involved proteins cause the xeroderma pigmentosum (XP) cancer predisposition syndrome. Although the general mechanism of the NER process is well studied, the function of the XPA protein, which is of central importance for successful NER, has remained enigmatic. It is known, that XPA binds kinked DNA structures and that it interacts also with DNA duplexes containing certain lesions, but the mechanism of interactions is unknown. Here we present two crystal structures of the DNA binding domain (DBD) of the yeast XPA homolog Rad14 bound to DNA with either a cisplatin lesion (1,2-GG) or an acetylaminofluorene adduct (AAF-dG). In the structures, we see that two Rad14 molecules bind to the duplex, which induces DNA melting of the duplex remote from the lesion. Each monomer interrogates the duplex with a β-hairpin, which creates a 13mer duplex recognition motif additionally characterized by a sharp 70° DNA kink at the position of the lesion. Although the 1,2-GG lesion stabilizes the kink due to the covalent fixation of the crosslinked dG bases at a 90° angle, the AAF-dG fully intercalates into the duplex to stabilize the kinked structure.
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