scholarly journals Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates

2017 ◽  
Vol 292 (41) ◽  
pp. 16847-16857 ◽  
Author(s):  
Norie Sugitani ◽  
Markus W. Voehler ◽  
Michelle S. Roh ◽  
Agnieszka M. Topolska-Woś ◽  
Walter J. Chazin
Keyword(s):  
Dna Binding ◽  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Human Factor ◽  
Excision Repair ◽  
Complementation Group ◽  
Nucleotide Excision ◽  
Group A ◽  
Insight Into

scholarly journals The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair

2020 ◽  
Vol 48 (17) ◽  
pp. 9943-9958
Author(s):  
Rocío González-Corrochano ◽  
Federico M Ruiz ◽  
Nicholas M I Taylor ◽  
Sonia Huecas ◽  
Srdja Drakulic ◽  
...  
Keyword(s):  
Dna Binding ◽  
Xeroderma Pigmentosum ◽  
Mutational Analysis ◽  
Excision Repair ◽  
Genetic Diseases ◽  
Complementation Group ◽  
Repair System ◽  
High Plasticity ◽  
Starting Point ◽  
Nucleotide Excision

Abstract Nucleotide excision repair (NER) is an essential pathway to remove bulky lesions affecting one strand of DNA. Defects in components of this repair system are at the ground of genetic diseases such as xeroderma pigmentosum (XP) and Cockayne syndrome (CS). The XP complementation group G (XPG) endonuclease cleaves the damaged DNA strand on the 3′ side of the lesion coordinated with DNA re-synthesis. Here, we determined crystal structures of the XPG nuclease domain in the absence and presence of DNA. The overall fold exhibits similarities to other flap endonucleases but XPG harbors a dynamic helical arch that is uniquely oriented and defines a gateway. DNA binding through a helix-2-turn-helix motif, assisted by one flanking α-helix on each side, shows high plasticity, which is likely relevant for DNA scanning. A positively-charged canyon defined by the hydrophobic wedge and β-pin motifs provides an additional DNA-binding surface. Mutational analysis identifies helical arch residues that play critical roles in XPG function. A model for XPG participation in NER is proposed. Our structures and biochemical data represent a valuable tool to understand the atomic ground of XP and CS, and constitute a starting point for potential therapeutic applications.

scholarly journals High-Mobility Group A1 Proteins Inhibit Expression of Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A

2007 ◽  
Vol 67 (13) ◽  
pp. 6044-6052 ◽  
Author(s):  
Jennifer E. Adair ◽  
Scott C. Maloney ◽  
Gregory A. Dement ◽  
Kelsey J. Wertzler ◽  
Michael J. Smerdon ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
High Mobility ◽  
High Mobility Group ◽  
Nucleotide Excision ◽  
Group A ◽  
Repair Factor ◽  
Xeroderma Pigmentosum Group A ◽  
Nucleotide Excision Repair Factor
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