Damage sensor role of UV-DDB during base excision repair

被引：0

作者：

Sunbok Jang

Namrata Kumar

Emily C. Beckwitt

Muwen Kong

Elise Fouquerel

Vesna Rapić-Otrin

Rajendra Prasad

Simon C. Watkins

Cindy Khuu

Chandrima Majumdar

Sheila S. David

Samuel H. Wilson

Marcel P. Bruchez

Patricia L. Opresko

Bennett Van Houten

机构：

[1] University of Pittsburgh School of Medicine,Department of Pharmacology and Chemical Biology

[2] University of Pittsburgh,UPMC Hillman Cancer Center

[3] University of Pittsburgh School of Medicine,Molecular Genetics and Developmental Biology Graduate Program

[4] University of Pittsburgh School of Medicine,Department of Microbiology and Molecular Genetics

[5] Carnegie Mellon University and University of Pittsburgh,Molecular Biophysics and Structural Biology Graduate Program

[6] University of Pittsburgh School of Public Health,Environmental and Occupational Health

[7] Genomic Integrity & Structural Biology Laboratory,Center for Biologic Imaging

[8] National Institute of Environmental Health Sciences,Department of Chemistry

[9] NIH,Biochemistry, Molecular, Cellular and Developmental Graduate Group

[10] University of Pittsburgh,Molecular Biosensor and Imaging Center

[11] University of California,Department of Biological Sciences

[12] Davis,Department of Chemistry

[13] University of California,Department of Biochemistry and Molecular Biophysics

[14] Davis,Department of Biochemistry and Molecular Biology

[15] Carnegie Mellon University,undefined

[16] Carnegie Mellon University,undefined

[17] Carnegie Mellon University,undefined

[18] Columbia University,undefined

[19] Thomas Jefferson University and Sydney Kimmel Medical College,undefined

来源：

Nature Structural & Molecular Biology | 2019年 / 26卷

关键词：

D O I：

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中图分类号：

学科分类号：

摘要：

UV-DDB, a key protein in human global nucleotide excision repair (NER), binds avidly to abasic sites and 8-oxo-guanine (8-oxoG), suggesting a noncanonical role in base excision repair (BER). We investigated whether UV-DDB can stimulate BER for these two common forms of DNA damage, 8-oxoG and abasic sites, which are repaired by 8-oxoguanine glycosylase (OGG1) and apurinic/apyrimidinic endonuclease (APE1), respectively. UV-DDB increased both OGG1 and APE1 strand cleavage and stimulated subsequent DNA polymerase β-gap filling activity by 30-fold. Single-molecule real-time imaging revealed that UV-DDB forms transient complexes with OGG1 or APE1, facilitating their dissociation from DNA. Furthermore, UV-DDB moves to sites of 8-oxoG repair in cells, and UV-DDB depletion sensitizes cells to oxidative DNA damage. We propose that UV-DDB is a general sensor of DNA damage in both NER and BER pathways, facilitating damage recognition in the context of chromatin.

引用

页码：695 / 703

页数：8

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