| http://purl.uniprot.org/citations/32302101 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32302101 | http://www.w3.org/2000/01/rdf-schema#comment | "The interplay between nucleotide excision repair (NER) and base excision repair (BER) of nonbulky, oxidatively generated DNA lesions has long been a subject of significant interest. The hydantoin oxidation products of 8-oxoguanine, spiroiminodihydantoin (Sp) and 5-guanidinohydantoin (Gh), are substrates of both BER and NER in HeLa cell extracts and human cells [Shafirovich, V., et al. (2019) Chem. Res. Toxicol. 32, 753-761]. The primary factor that recognizes DNA lesions is the DNA damage-sensing factor XPC-RAD23B (XPC), while the glycosylase NEIL1 is known to remove Gh and Sp lesions from double-stranded DNA. It is shown here that in aqueous solutions containing nanomolar concentrations of proteins, XPC and NEIL1 compete for binding to 147-mer oligonucleotide duplexes that contain single Gh or Sp lesions under conditions of [protein] ≫ [DNA], thus inhibiting the rate of BER catalyzed by NEIL1. The non-covalently bound NEIL1 molecules can be displaced by XPC at concentration ratios R = [XPC]/[NEIL1] > 0.2, while full displacement of NEIL1 is observed at R ≥ 0.5. In the absence of XPC and under single-turnover conditions, only the burst phase is observable. However, with a progressive increase in the XPC concentration, the amplitude of the burst phase decreases gradually, and a slower time-dependent phase of incision product formation manifests itself with rate constants of 3.0 × 10-3 s-1 (Gh) and 0.90 × 10-3 s-1 (Sp). These slow kinetics are attributed to the dissociation of XPC-DNA complexes that allow for the rebinding of NEIL1 to the temporarily exposed Gh or Sp lesions, and the incisions observed under these steady-state conditions."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.biochem.0c00080"xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/author | "Min J.H."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/author | "Geacintov N.E."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/author | "Shim Y."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/author | "Shafirovich V."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/author | "Kolbanovskiy M."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/pages | "1728-1736"xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/title | "Inhibition of Excision of Oxidatively Generated Hydantoin DNA Lesions by NEIL1 by the Competitive Binding of the Nucleotide Excision Repair Factor XPC-RAD23B."xsd:string |
| http://purl.uniprot.org/citations/32302101 | http://purl.uniprot.org/core/volume | "59"xsd:string |
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