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

Abstract：

: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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Akita M,Tak YS,Shimura T,Matsumoto S,Okuda-Shimizu Y,Shimizu Y,Nishi R,Saitoh H,Iwai S,Mori T,Ikura T,Sakai W,Hanaoka F,Sugasawa K

doi

10.1038/srep10984

subject

Has Abstract

pub_date

2015-06-04 00:00:00

pages

10984

issn

2045-2322

pii

srep10984

journal_volume

5

pub_type

杂志文章

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