ArticleThe Journal of biological chemistry2013
Comparative analysis of interaction of human and yeast DNA damage recognition complexes with damaged DNA in nucleotide excision repair.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- DNA adduct formation in Saccharomyces cerevisiae following exposure to environmental pollutants, as in vivo model for molecular toxicity studies.World journal of microbiology & biotechnology · 2024Article
- Conformation-dependent lesion bypass of bulky arylamine-dG adducts generated from 2-nitrofluorene in epigenetic sequence contexts.Nucleic acids research · 2023Article
- Article
- Structural modeling and analyses of genetic variations in the human XPC nucleotide excision repair protein.Journal of biomolecular structure & dynamics · 2023Article
- RPA and XPA interaction with DNA structures mimicking intermediates of the late stages in nucleotide excision repair.PloS one · 2018Article
- Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process.Molecular cell · 2016Article
- Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation.Cellular and molecular life sciences : CMLS · 2016Review
- XPC: Going where no DNA damage sensor has gone before.DNA repair · 2015Review
- Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA).Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Nucleotide excision repair factor XPC-RAD23B is poly(ADP-ribosylated) by the poly(ADP-ribose) polymerase 1.Doklady. Biochemistry and biophysics · 2015Article
- The relationships between XPC binding to conformationally diverse DNA adducts and their excision by the human NER system: is there a correlation?DNA repair · 2014Article
- Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.The Journal of biological chemistry · 2014Article
- Autonomous inhibition of apoptosis correlates with responsiveness of colon carcinoma cell lines to ciglitazone.PloS one · 2014Article
- Molecular mechanism of global genome nucleotide excision repair.Acta naturae · 2014Article
- The intertwined roles of transcription and repair proteins.Molecular cell · 2013Review
- Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human XPC-RAD23B complex and its yeast ortholog, Rad4-Rad23, are the primary initiators of global genome nucleotide excision repair. The interaction of these proteins with damaged DNA was analyzed using model DNA duplexes containing a single fluorescein-substituted dUMP analog as a lesion. An electrophoretic mobility shift assay revealed similarity between human and yeast proteins in DNA binding. Quantitative analyses of XPC/Rad4 binding to the model DNA structures were performed by fluorescent depolarization measurements. XPC-RAD23B and Rad4-Rad23 proteins demonstrate approximately equal binding affinity to the damaged DNA duplex (K(D) ∼ (0.5 ± 0.1) and (0.6 ± 0.3) nM, respectively). Using photoreactive DNA containing 5-iodo-dUMP in defined positions, XPC/Rad4 location on damaged DNA was shown. Under conditions of equimolar binding to DNA both proteins exhibited the highest level of cross-links to 5I-dUMP located exactly opposite the damaged nucleotide. The positioning of the XPC and Rad4 proteins on damaged DNA by photocross-linking footprinting is consistent with x-ray analysis of the Rad4-DNA crystal complex. The identity of the XPC and Rad4 location illustrates the common principles of structure organization of DNA damage-scanning proteins from different Eukarya organisms.
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