Faculty Opinions recommendation of A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex.

2003 ◽  
Author(s):  
Errol C Friedberg
Keyword(s):  
Dna Damage ◽  
Molecular Mechanism ◽  
Protein Complex ◽  
Xeroderma Pigmentosum ◽  
C Protein ◽  
Damage Recognition ◽  
Dna Damage Recognition

scholarly journals Dynamic two-stage mechanism of versatile DNA damage recognition by xeroderma pigmentosum group C protein

2010 ◽  
Vol 685 (1-2) ◽  
pp. 21-28 ◽  
Author(s):  
Flurina C. Clement ◽  
Ulrike Camenisch ◽  
Jia Fei ◽  
Nina Kaczmarek ◽  
Nadine Mathieu ◽  
...  
Keyword(s):  
Dna Damage ◽  
Xeroderma Pigmentosum ◽  
Two Stage ◽  
C Protein ◽  
Damage Recognition ◽  
Dna Damage Recognition

scholarly journals Functional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein

2015 ◽  
Vol 43 (3) ◽  
pp. 1700-1713 ◽  
Author(s):  
Syota Matsumoto ◽  
Eric S. Fischer ◽  
Takeshi Yasuda ◽  
Naoshi Dohmae ◽  
Shigenori Iwai ◽  
...  
Keyword(s):  
Dna Damage ◽  
Xeroderma Pigmentosum ◽  
C Protein ◽  
Damage Recognition ◽  
Functional Regulation ◽  
Dna Damage Recognition

scholarly journals Centrin 2 Stimulates Nucleotide Excision Repair by Interacting with Xeroderma Pigmentosum Group C Protein

2005 ◽  
Vol 25 (13) ◽  
pp. 5664-5674 ◽  
Author(s):  
Ryotaro Nishi ◽  
Yuki Okuda ◽  
Eriko Watanabe ◽  
Toshio Mori ◽  
Shigenori Iwai ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Physical Interaction ◽  
C Protein ◽  
Damage Recognition ◽  
C Terminus ◽  
Nucleotide Excision ◽  
Dna Damage Recognition

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.

scholarly journals Damage-recognition proteins as a potential indicator of DNA-damage-mediated sensitivity or resistance of human cells to ultraviolet radiation

1992 ◽  
Vol 282 (1) ◽  
pp. 203-207 ◽  
Author(s):  
C C K Chao
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Hela Cells ◽  
Xeroderma Pigmentosum ◽  
Cross Linking ◽  
Damage Recognition ◽  
Modified Dna ◽  
Potential Indicator ◽  
Recognition Protein ◽  
Dna Damage Recognition

We have previously identified damage-recognition proteins that bind to cisplatin[cis-diamminedichloroplatinum(II), a DNA cross-linking agent]- or u.v.-modified DNA in HeLa cells [Chao, Huang, Huang & Lin-Chao (1991) Mol. Cell. Biol. 11, 2075-2080; Chao, Huang, Lee & Lin-Chao (1991) Biochem. J. 277, 875-878]. In the present study we compared damage-recognition proteins in cells expressing different sensitivities to DNA damage. An increase in damage-recognition proteins and an enhancement of plasmid re-activation were detected in HeLa cells resistant to cisplatin and u.v. However, repair-defective cells derived from xeroderma-pigmentosum (a rare skin disease) patients did not express less cisplatin damage-recognition proteins than repair-competent cells, suggesting that damage-recognition-protein expression may not be related to DNA repair. By contrast, cells resistant to DNA damage consistently expressed high levels of u.v.-modified-DNA damage-recognition proteins. The results support the notion that u.v. damage-recognition proteins are different from those that bind to cisplatin. These findings also suggest that the damage-recognition proteins identified could be used as potential indicators of the sensitivity or resistance of cells to u.v.

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