ArticleNucleic acids research2004
Roles of Rad23 protein in yeast nucleotide excision repair.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 73 citations in OpenAlex.
- Domains in Action: Understanding Ddi1's Diverse Functions in the Ubiquitin-Proteasome System.International journal of molecular sciences · 2024Review
- Genetic polymorphisms as potential pharmacogenetic biomarkers for platinum-based chemotherapy in non-small cell lung cancer.Molecular biology reports · 2024Review
- Divergent roles of Rad4 and Rad23 homologs inApplied and environmental microbiology · 2023Article
- Article
- Comparative Roles of Rad4A and Rad4B in Photoprotection ofJournal of fungi (Basel, Switzerland) · 2023Article
- Structural modeling and analyses of genetic variations in the human XPC nucleotide excision repair protein.Journal of biomolecular structure & dynamics · 2023Article
- Rad1 and Rad10 Tied to Photolyase Regulators Protect Insecticidal Fungal Cells from Solar UV Damage by Photoreactivation.Journal of fungi (Basel, Switzerland) · 2022Article
- BmNPV Orf 65 (Bm65) Is Identified as an Endonuclease Directly Facilitating UV-Induced DNA Damage Repair.Journal of virology · 2022Article
- Altitudinal Heterogeneity of UV Adaptation inJournal of fungi (Basel, Switzerland) · 2021Article
- New Insights inToxins · 2020Article
- Photoprotective Role of Photolyase-Interacting RAD23 and Its Pleiotropic Effect on the Insect-Pathogenic Fungus Beauveria bassiana.Applied and environmental microbiology · 2020Article
- Nucleotide Excision Repair Protein Rad23 Regulates Cell Virulence Independent of Rad4 in Candida albicans.mSphere · 2020Article
- Comparative Transcriptome Analyses ofFrontiers in microbiology · 2020Article
- Article
- Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation.Cellular and molecular life sciences : CMLS · 2016Review
- Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers.Frontiers in genetics · 2016Review
- Autophagy positively regulates DNA damage recognition by nucleotide excision repair.Autophagy · 2016Article
- XPC: Going where no DNA damage sensor has gone before.DNA repair · 2015Review
- Architecture of the human XPC DNA repair and stem cell coactivator complex.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- UV induced ubiquitination of the yeast Rad4-Rad23 complex promotes survival by regulating cellular dNTP pools.Nucleic acids research · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Nucleotide excision repair (NER) removes many different types of DNA lesions. Most NER proteins are indispensable for repair. In contrast, the yeast Rad23 represents a class of accessory NER proteins, without which NER activity is reduced but not eliminated. In mammals, the complex of HR23B (Rad23 homolog) and XPC (yeast Rad4 homolog) has been suggested to function in the damage recognition step of NER. However, the precise function of Rad23 or HR23B in NER remains unknown. Recently, it was suggested that the primary function of RAD23 protein in NER is its stabilization of XPC protein. Here, we tested the significance of Rad23-mediated Rad4 stabilization in NER, and analyzed the repair and biochemical activities of purified yeast Rad23 protein. Cellular Rad4 was indeed stabilized by Rad23 in the absence of DNA damage. Persistent overexpression of Rad4 in rad23 mutant cells, however, largely failed to complement the ultraviolet sensitivity of the mutant. Consistently, deficient NER in rad23 mutant cell extracts could not be complemented by purified Rad4 protein in vitro. In contrast, partial complementation was observed with purified Rad23 protein. Specific complementation to the level of wild-type repair was achieved by adding purified Rad23 together with small amounts of Rad4 protein to rad23 mutant cell extracts. Purified Rad23 protein was unable to bind to DNA, but stimulated the binding activity of purified Rad4 protein to N-acetyl-2-aminofluorene-damaged DNA. These results support two roles of Rad23 protein in NER: (i) its direct participation in the repair biochemistry, possibly due to its stimulatory activity on Rad4-mediated damage binding/recognition; and (ii) its stabilization of cellular Rad4 protein.
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