SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair

The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in v...

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Bibliographic Details
Published in:Scientific reports 2015-06, Vol.5 (1), p.10984-10984, Article 10984
Main Authors: Akita, Masaki, Tak, Yon-Soo, Shimura, Tsutomu, Matsumoto, Syota, Okuda-Shimizu, Yuki, Shimizu, Yuichiro, Nishi, Ryotaro, Saitoh, Hisato, Iwai, Shigenori, Mori, Toshio, Ikura, Tsuyoshi, Sakai, Wataru, Hanaoka, Fumio, Sugasawa, Kaoru
Format: Article
Language:English
Subjects:
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C protein
Cell Line
Deoxyribonucleic acid
DNA
DNA Damage
DNA Repair
DNA-binding protein
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Humanities and Social Sciences
Humans
Mammalian cells
multidisciplinary
Mutation
Nucleotide excision repair
Protein Binding
Proteins
Science
SUMO protein
SUMO-1 Protein - metabolism
Sumoylation
Ubiquitin
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitination - radiation effects
Ultraviolet radiation
Ultraviolet Rays
Xeroderma pigmentosum
XPC protein
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Summary:The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep10984