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

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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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Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K., van der Spek, P.J., Bootsma, D.·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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Background
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See all 400

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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