Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.

Masutani, C.; Sugasawa, K.; Yanagisawa, J.; Sonoyama, T.; Ui, M.; Enomoto, T.; Takio, K.; Tanaka, K.; van der Spek, P.J.; Bootsma, D.

doi:10.1002/j.1460-2075.1994.tb06452.x

Cited by 400DNA Repair MechanismsUbiquitin and proteasome pathwaysNuclear Structure and Function

Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.

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Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K. +2 more·1994·The EMBO Journal

DOI 10.1002/j.1460-2075.1994.tb06452.xPMC PMC395023

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Abstract

Complementation group C of xeroderma pigmentosum (XP) represents one of the most common forms of this cancer-prone DNA repair syndrome. The primary defect is located in the subpathway of the nucleotide excision repair system, dealing with the removal of lesions from the non-transcribing sequences ('genome-overall' repair). Here we report the purification to homogeneity and subsequent cDNA cloning of a repair complex by in vitro complementation of the XP-C defect in a cell-free repair system containing UV-damaged SV40 minichromosomes. The complex has a high affinity for ssDNA and consists of two tightly associated proteins of 125 and 58 kDa. The 125 kDa subunit is an N-terminally extended version of previously reported XPCC gene product which is thought to represent the human homologue of the Saccharomyces cerevisiae repair gene RAD4. The 58 kDa species turned out to be a human homologue of yeast RAD23. Unexpectedly, a second human counterpart of RAD23 was identified. All RAD23 derivatives share a ubiquitin-like N-terminus. The nature of the XP-C defect implies that the complex exerts a unique function in the genome-overall repair pathway which is important for prevention of skin cancer.

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The hHR23B-XPC complex, or XPC alone, binds UV-induced single-stranded and double-stranded DNA with similar high affinity, prefers DNA containing various lesions, and can bind small bubble structures with or without a lesion.
“hHR23B-XPC complex or only XPC exhibits a similar high affinity for both UV-induced single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) [230, 259], preferentially binds to DNA with various lesions [259] and even to small bubble structures with or without a lesion [260].”
From Molecular Mechanisms of Ultraviolet Radiation‐Induced DNA Damage and Repair (2010) · cites this paper as [230]
The Results report that the XP-C–HHR23B complex bound strongly to a single-stranded DNA-cellulose column. The Discussion says this indicates high affinity for ssDNA but explicitly leaves open which component is responsible. The paper does not establish similarly high affinity for UV-damaged double-stranded DNA or for XPC alone; the citing sentence assigns the lesion and bubble claims to other references. (LLM, conf=0.88)
Experimental — accuracy not yet measured
hHR23A and hHR23B each carry a ubiquitin-like domain at their amino terminus.
“Both hHR23A and -B harbor a ubiquitin-like moiety at their amino terminus [230].”
From Molecular Mechanisms of Ultraviolet Radiation‐Induced DNA Damage and Repair (2010) · cites this paper as [230]

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XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes
van der Spek, P. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.13.2551 · Cited by 119 · see citing works
Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2
Scherly, D., Nouspikel, T. P., Corlet, J., Ucla, C., Bairoch, A., & Clarkson, S. G. (1993) · Nature · doi:10.1038/363182a0 · Cited by 203 · see citing works
RAD25(SSL2), a yeast homolog of the human xeroderma pigmentosum group B DNA repair gene, is essential for viability.
Park, R., Guzder, S. N., Koken, M., Jaspers-Dekker, I., Weeda, G., Hoeijmakers, J. H. J., Prakash, S., & Prakash, L. (1992) · RePub (Erasmus University Rotterdam)
DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells.
Shivji, M. K. K., Eker, A. P. M., & Wood, R. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31709-x · Cited by 90 · see citing works

Authors: Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K., van der Spek, P. J., & Bootsma, D.
Affiliations: RIKEN (JP)
ORCID: Masutani, C.
Sugasawa, K.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1994-04-01
Volume: 13
Issue: 8
Pages: 1831-1843
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1994.tb06452.x
PMC: PMC395023
OpenAlex: W1005028082
Cited by: 400
References: 70
Citations by year: 2026: 5 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 5 · 2021: 7 · 2020: 8 · 2019: 9 · 2018: 5 · 2017: 7 · 2016: 13 · 2015: 9 · 2014: 7 · 2013: 5 · 2012: 9
FWCI: 9.75
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
Funders: Cosmetology Research Foundation
RIKEN
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: xeroderma pigmentosum group C, nucleotide excision repair, Rad23, Rad4, UV-damaged DNA, single-stranded DNA binding, cDNA cloning, protein complex purification, skin cancer prevention, SV40 minichromosomes
MeSH terms: Amino Acid Sequence, Base Sequence, DNA Damage, DNA Repair, DNA-Binding Proteins, DNA, Viral, Fungal Proteins, HeLa Cells, Humans, Models, Molecular, Molecular Sequence Data, Transglutaminases, Simian virus 40, Ubiquitins, Ultraviolet Rays, Sequence Homology, Amino Acid, DNA, Complementary, Schizosaccharomyces pombe Proteins, DNA Repair Enzymes

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Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.

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