ArticleThe Journal of biological chemistry2011
Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA.
Article in The Journal of biological chemistry, 2011. 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, 41 citations in OpenAlex.
- Review
- The mechanism and clinical application of DNA damage repair inhibitors combined with immune checkpoint inhibitors in the treatment of urologic cancer.Frontiers in cell and developmental biology · 2023Review
- 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
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Xeroderma pigmentosum A homolog fromJournal of biosciences · 2021Article
- Article
- Molecular Mechanisms of Arsenic-Induced Disruption of DNA Repair.Chemical research in toxicology · 2020Review
- A key interaction with RPA orients XPA in NER complexes.Nucleic acids research · 2020Article
- Characterizing the Binding Interactions between DNA-Binding Proteins, XPA and XPE: A Molecular Dynamics Approach.ACS omega · 2018Article
- RPA and XPA interaction with DNA structures mimicking intermediates of the late stages in nucleotide excision repair.PloS one · 2018Article
- Design and Structure-Guided Development of Novel Inhibitors of the Xeroderma Pigmentosum Group A (XPA) Protein-DNA Interaction.Journal of medicinal chemistry · 2017Article
- XPA: A key scaffold for human nucleotide excision repair.DNA repair · 2016Review
- HMGB1 interacts with XPA to facilitate the processing of DNA interstrand crosslinks in human cells.Nucleic acids research · 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
- The RASSF1A tumor suppressor regulates XPA-mediated DNA repair.Molecular and cellular biology · 2015Article
- RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response.Cell research · 2015Review
- Coordinated regulation of XPA stability by ATR and HERC2 during nucleotide excision repair.Oncogene · 2014Article
- Nucleotide excision repair in eukaryotes.Cold Spring Harbor perspectives in biology · 2013Review
- In silico characterization of a novel pathogenic deletion mutation identified in XPA gene in a Pakistani family with severe xeroderma pigmentosum.Journal of biomedical science · 2013Article
- Human single-stranded DNA binding proteins are essential for maintaining genomic stability.BMC molecular biology · 2013Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The xeroderma pigmentosum group A protein (XPA) is a core component of nucleotide excision repair (NER). To coordinate early stage NER, XPA interacts with various proteins, including replication protein A (RPA), ERCC1, DDB2, and TFIIH, in addition to UV-damaged or chemical carcinogen-damaged DNA. In this study, we investigated the effects of mutations in the RPA binding regions of XPA on XPA function in NER. XPA binds through an N-terminal region to the middle subunit (RPA32) of the RPA heterotrimer and through a central region that overlaps with its damaged DNA binding region to the RPA70 subunit. In cell-free NER assays, an N-terminal deletion mutant of XPA showed loss of binding to RPA32 and reduced DNA repair activity, but it could still bind to UV-damaged DNA and RPA. In contrast, amino acid substitutions in the central region reduced incisions at the damaged site in the cell-free NER assay, and four of these mutants (K141A, T142A, K167A, and K179A) showed reduced binding to RPA70 but normal binding to damaged DNA. Furthermore, mutants that had one of the four aforementioned substitutions and an N-terminal deletion exhibited lower DNA incision activity and binding to RPA than XPA with only one of these substitutions or the deletion. Taken together, these results indicate that XPA interaction with both RPA32 and RPA70 is indispensable for NER reactions.
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