ArticleMolecular and cellular biology1997
Identification and characterization of XPC-binding domain of hHR23B.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.
- A meta-analysis of DNA repair gene XPC polymorphisms and cancer risk.Journal of human genetics · 2008Pooled it
- The deubiquitinase OTUD1 orchestrates cisplatin chemosensitivity of non-small cell lung cancer through destabilizing RAD23B/XPC.Oncogene · 2025Article
- Domains in Action: Understanding Ddi1's Diverse Functions in the Ubiquitin-Proteasome System.International journal of molecular sciences · 2024Review
- A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases.Journal of molecular biology · 2023Article
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum-binding proteins in nucleotide excision repair.Protein science : a publication of the Protein Society · 2021Review
- XPC Polymorphism and Risk for Lung Cancer in North Indian Patients Treated with Platinum Based Chemotherapy and Its Association with Clinical Outcomes.Pathology oncology research : POR · 2018Article
- Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Scientific reports · 2016Article
- Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis.The Journal of biological chemistry · 2014Article
- Article
- Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.The Journal of biological chemistry · 2014Article
- A human XPC protein interactome--a resource.International journal of molecular sciences · 2013Article
- Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA.DNA repair · 2013Article
- Lack of recognition by global-genome nucleotide excision repair accounts for the high mutagenicity and persistence of aristolactam-DNA adducts.Nucleic acids research · 2012Article
- Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair.Journal of nucleic acids · 2010Article
- Stimulation of DNA Glycosylase Activities by XPC Protein Complex: Roles of Protein-Protein Interactions.Journal of nucleic acids · 2010Article
- Involvement of global genome repair, transcription coupled repair, and chromatin remodeling in UV DNA damage response changes during development.PLoS genetics · 2010Article
- Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.The Journal of biological chemistry · 2010Article
- Dissection of the molecular defects caused by pathogenic mutations in the DNA repair factor XPC.Molecular and cellular biology · 2008Article
- Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
hHR23B was originally isolated as a component of a protein complex that specifically complements nucleotide excision repair (NER) defects of xeroderma pigmentosum group C cell extracts in vitro and was identified as one of two human homologs of the Saccharomyces cerevisiae NER gene product Rad23. Recombinant hHR23B has previously been shown to significantly stimulate the NER activity of recombinant human XPC protein (rhXPC). In this study we identify and functionally characterize the XPC-binding domain of hHR23B protein. We prepared various internal as well as terminal deletion products of hHR23B protein in a His-tagged form and examined their binding with rhXPC by using nickel-chelating Sepharose. We demonstrate that a domain covering 56 amino acids of hHR23B is required for binding to rhXPC as well as for stimulation of in vitro NER reactions. Interestingly, a small polypeptide corresponding to the XPC-binding domain is sufficient to exert stimulation of XPC NER activity. Comparison with known crystal structures and analysis with secondary structure programs provided strong indications that the binding domain has a predominantly amphipathic alpha-helical character, consistent with evidence that the affinity with XPC is based on hydrophobic interactions. Our work shows that binding to XPC alone is required and sufficient for the role of hHR23B in in vitro NER but does not rule out the possibility that the protein has additional functions in vivo.
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