ArticleThe Journal of biological chemistry2017
Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- XPA confers ability of endonucleases to act processively and to incise damaged nucleosomal DNA.Experimental biology and medicine (Maywood, N.J.) · 2026Review
- 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
- Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An Active Learning Framework Improves Tumor Variant Interpretation.Cancer research · 2022Article
- In Vitro Assessment of the Genotoxic Hazard of Novel Hydroxamic Acid- and Benzamide-Type Histone Deacetylase Inhibitors (HDACi).International journal of molecular sciences · 2020Article
- XPA: DNA Repair Protein of Significant Clinical Importance.International journal of molecular sciences · 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
- 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
- Characterizing the Binding Interactions between DNA-Binding Proteins, XPA and XPE: A Molecular Dynamics Approach.ACS omega · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Xeroderma pigmentosum (XP) complementation group A (XPA) is an essential scaffolding protein in the multiprotein nucleotide excision repair (NER) machinery. The interaction of XPA with DNA is a core function of this protein; a number of mutations in the DNA-binding domain (DBD) are associated with XP disease. Although structures of the central globular domain of human XPA and data on binding of DNA substrates have been reported, the structural basis for XPA's DNA-binding activity remains unknown. X-ray crystal structures of the central globular domain of yeast XPA (Rad14) with lesion-containing DNA duplexes have provided valuable insights, but the DNA substrates used for this study do not correspond to the substrates of XPA as it functions within the NER machinery. To better understand the DNA-binding activity of human XPA in NER, we used NMR to investigate the interaction of its DBD with a range of DNA substrates. We found that XPA binds different single-stranded/double-stranded junction DNA substrates with a common surface. Comparisons of our NMR-based mapping of binding residues with the previously reported Rad14-DNA crystal structures revealed similarities and differences in substrate binding between XPA and Rad14. This includes direct evidence for DNA contacts to the residues extending C-terminally from the globular core, which are lacking in the Rad14 construct. Moreover, mutation of the XPA residue corresponding to Phe-262 in Rad14, previously reported as being critical for DNA binding, had only a moderate effect on the DNA-binding activity of XPA. The DNA-binding properties of several disease-associated mutations in the DBD were investigated. These results suggest that for XPA mutants exhibiting altered DNA-binding properties, a correlation exists between the extent of reduction in DNA-binding affinity and the severity of symptoms in XP patients.
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