scholarly journals Checkpoint Kinase ATR Promotes Nucleotide Excision Repair of UV-induced DNA Damage via Physical Interaction with Xeroderma Pigmentosum Group A

2009 ◽  
Vol 284 (36) ◽  
pp. 24213-24222 ◽  
Author(s):  
Steven M. Shell ◽  
Zhengke Li ◽  
Nikolozi Shkriabai ◽  
Mamuka Kvaratskhelia ◽  
Chris Brosey ◽  
...  
2007 ◽  
Vol 67 (13) ◽  
pp. 6044-6052 ◽  
Author(s):  
Jennifer E. Adair ◽  
Scott C. Maloney ◽  
Gregory A. Dement ◽  
Kelsey J. Wertzler ◽  
Michael J. Smerdon ◽  
...  

2010 ◽  
Vol 38 (22) ◽  
pp. 8083-8094 ◽  
Author(s):  
Yuliya S. Krasikova ◽  
Nadejda I. Rechkunova ◽  
Ekaterina A. Maltseva ◽  
Irina O. Petruseva ◽  
Olga I. Lavrik

2005 ◽  
Vol 25 (13) ◽  
pp. 5664-5674 ◽  
Author(s):  
Ryotaro Nishi ◽  
Yuki Okuda ◽  
Eriko Watanabe ◽  
Toshio Mori ◽  
Shigenori Iwai ◽  
...  

ABSTRACT Xeroderma pigmentosum group C (XPC) protein plays a key role in DNA damage recognition in global genome nucleotide excision repair (NER). The protein forms in vivo a heterotrimeric complex involving one of the two human homologs of Saccharomyces cerevisiae Rad23p and centrin 2, a centrosomal protein. Because centrin 2 is dispensable for the cell-free NER reaction, its role in NER has been unclear. Binding experiments with a series of truncated XPC proteins allowed the centrin 2 binding domain to be mapped to a presumed α-helical region near the C terminus, and three amino acid substitutions in this domain abrogated interaction with centrin 2. Human cell lines stably expressing the mutant XPC protein exhibited a significant reduction in global genome NER activity. Furthermore, centrin 2 enhanced the cell-free NER dual incision and damaged DNA binding activities of XPC, which likely require physical interaction between XPC and centrin 2. These results reveal a novel vital function for centrin 2 in NER, the potentiation of damage recognition by XPC.


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