ArticleJournal of the American Chemical Society2014
Redefining the DNA-binding domain of human XPA.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Cross-species investigation into the requirement of XPA for nucleotide excision repair.Nucleic acids research · 2024Article
- A disease-associated XPA allele interferes with TFIIH binding and primarily affects transcription-coupled nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Xeroderma pigmentosum A homolog fromJournal of biosciences · 2021Article
- 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
- Association of humanCancer cell international · 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
- Article
- 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
- Progerin sequestration of PCNA promotes replication fork collapse and mislocalization of XPA in laminopathy-related progeroid syndromes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Photonic-plasmonic hybrid single-molecule nanosensor measures the effect of fluorescent labels on DNA-protein dynamics.Science advances · 2017Article
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Xeroderma pigmentosum complementation group A (XPA) protein plays a critical role in the repair of DNA damage via the nucleotide excision repair (NER) pathway. XPA serves as a scaffold for NER, interacting with several other NER proteins as well as the DNA substrate. The critical importance of XPA is underscored by its association with the most severe clinical phenotypes of the genetic disorder Xeroderma pigmentosum. Many of these disease-associated mutations map to the XPA(98-219) DNA-binding domain (DBD) first reported ~20 years ago. Although multiple solution NMR structures of XPA(98-219) have been determined, the molecular basis for the interaction of this domain with DNA is only poorly characterized. In this report, we demonstrate using a fluorescence anisotropy DNA-binding assay that the previously reported XPA DBD binds DNA with substantially weaker affinity than the full-length protein. In-depth analysis of the XPA sequence suggested that the original DBD construct lacks critical basic charge and helical elements at its C-terminus. Generation and analysis of a series of C-terminal extensions beyond residue 219 yielded a stable, soluble human XPA(98-239) construct that binds to a Y-shaped ssDNA-dsDNA junction and other substrates with the same affinity as the full-length protein. Two-dimensional (15)N-(1)H NMR suggested XPA(98-239) contains the same globular core as XPA98-219 and likely undergoes a conformational change upon binding DNA. Together, our results demonstrate that the XPA DBD should be redefined and that XPA(98-239) is a suitable model to examine the DNA binding activity of human XPA.
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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.