The Nucleotide Excision Repair of DNA in Human Cells and Its Association with Xeroderma Pigmentosum

2008 ◽  
pp. 113-119 ◽  
Author(s):  
Alexei Gratchev
Keyword(s):  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Human Cells ◽  
Nucleotide Excision

scholarly journals Xeroderma Pigmentosum Diagnosis Using a Flow Cytometry-Based Nucleotide Excision Repair Assay

2018 ◽  
Vol 138 (2) ◽  
pp. 467-470 ◽  
Author(s):  
Eiji Nakano ◽  
Seiji Takeuchi ◽  
Ryusuke Ono ◽  
Mariko Tsujimoto ◽  
Taro Masaki ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Nucleotide Excision

scholarly journals Nucleotide Excision Repair in Human Cells

2013 ◽  
Vol 288 (29) ◽  
pp. 20918-20926 ◽  
Author(s):  
Jinchuan Hu ◽  
Jun-Hyuk Choi ◽  
Shobhan Gaddameedhi ◽  
Michael G. Kemp ◽  
Joyce T. Reardon ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Genomic Dna ◽  
Excision Repair ◽  
Human Cells ◽  
Naked Dna ◽  
Nucleotide Excision ◽  
Uv Photoproducts ◽  
Mutant Cells

Nucleotide excision repair is the sole mechanism for removing the major UV photoproducts from genomic DNA in human cells. In vitro with human cell-free extract or purified excision repair factors, the damage is removed from naked DNA or nucleosomes in the form of 24- to 32-nucleotide-long oligomers (nominal 30-mer) by dual incisions. Whether the DNA damage is removed from chromatin in vivo in a similar manner and what the fate of the excised oligomer was has not been known previously. Here, we demonstrate that dual incisions occur in vivo identical to the in vitro reaction. Further, we show that transcription-coupled repair, which operates in the absence of the XPC protein, also generates the nominal 30-mer in UV-irradiated XP-C mutant cells. Finally, we report that the excised 30-mer is released from the chromatin in complex with the repair factors TFIIH and XPG. Taken together, our results show the congruence of in vivo and in vitro data on nucleotide excision repair in humans.

Xeroderma pigmentosum complementation group A protein is driven to nucleotide excision repair sites by the electrostatic potential of distorted DNA

DNA Repair ◽  
2007 ◽  
Vol 6 (12) ◽  
pp. 1819-1828 ◽  
Author(s):  
Ulrike Camenisch ◽  
Ramiro Dip ◽  
Mirela Vitanescu ◽  
Hanspeter Naegeli
Keyword(s):  
Nucleotide Excision Repair ◽  
Electrostatic Potential ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Complementation Group ◽  
Nucleotide Excision ◽  
Group A

O V A.1 Nucleotide excision repair mechanism in human cells: Analysis by in vitro assays

1997 ◽  
Vol 379 (1) ◽  
pp. S33
Author(s):  
Bernard Salles ◽  
Patrick Calsou ◽  
Philippe Frit ◽  
Ruo-Ya Li ◽  
Catherine Muller ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Human Cells ◽  
In Vitro Assays ◽  
Repair Mechanism ◽  
Nucleotide Excision

Nucleotide Excision Repair in the Three Domains of Life

2011 ◽  
Vol 2 (1) ◽  
Author(s):  
David A Farnell
Keyword(s):  
Dna Repair ◽  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Human Diseases ◽  
Repair Pathway ◽  
Functional Conservation ◽  
Wide Range ◽  
Nucleotide Excision ◽  
Domains Of Life

Nucleotide excision repair (NER) is a vital DNA repair pathway which acts on a wide range of helix-distorting lesions. The importance of this pathway is highlighted by its functional conservation throughout evolution and by several human diseases, such as xeroderma pigmentosum, which are caused by a defective NER pathway. This review summarizes the NER mechanisms present in all three domains of life: eukaryotes, bacteria, and archaea.

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.

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