scholarly journals Poly(ADP-ribose) Polymerase-1 (PARP-1) Is Required in Murine Cell Lines for Base Excision Repair of Oxidative DNA Damage in the Absence of DNA Polymerase β

2003 ◽  
Vol 278 (20) ◽  
pp. 18471-18477 ◽  
Author(s):  
Florence Le Page ◽  
Valérie Schreiber ◽  
Claudine Dhérin ◽  
Gilbert de Murcia ◽  
Serge Boiteux
Keyword(s):  
Dna Damage ◽  
Cell Lines ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Murine Cell ◽  
Base Excision ◽  
Parp 1

scholarly journals The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery

2005 ◽  
Vol 389 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Ekaterina SMIRNOVA ◽  
Magali TOUEILLE ◽  
Enni MARKKANEN ◽  
Ulrich HÜBSCHER
Keyword(s):  
Quality Control ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Flap Endonuclease 1 ◽  
Important Target ◽  
Dna Ligase I ◽  
Base Excision

The human checkpoint sensor and alternative clamp Rad9–Rad1–Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9–Rad1–Hus1 with MutY DNA glycosylase, DNA polymerase β and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9–Rad1–Hus1 complex, thus enhancing the quality control of DNA.

scholarly journals DNA polymerase β outperforms DNA polymerase γ in key mitochondrial base excision repair activities

DNA Repair ◽  
2021 ◽  
Vol 99 ◽  
pp. 103050
Author(s):  
Beverly A. Baptiste ◽  
Stephanie L. Baringer ◽  
Tomasz Kulikowicz ◽  
Joshua A. Sommers ◽  
Deborah L. Croteau ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Base Excision ◽  
Dna Polymerase Γ

scholarly journals Base excision repair and design of small molecule inhibitors of human DNA polymerase β

2010 ◽  
Vol 67 (21) ◽  
pp. 3633-3647 ◽  
Author(s):  
Samuel H. Wilson ◽  
William A. Beard ◽  
David D. Shock ◽  
Vinod K. Batra ◽  
Nisha A. Cavanaugh ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Small Molecule ◽  
Base Excision Repair ◽  
Small Molecule Inhibitors ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Base Excision

DNA Polymerase β Promotes Recruitment of DNA Ligase IIIα−XRCC1 to Sites of Base Excision Repair

Biochemistry ◽  
2005 ◽  
Vol 44 (31) ◽  
pp. 10613-10619 ◽  
Author(s):  
Jason L. Parsons ◽  
Irina I. Dianova ◽  
Sarah L. Allinson ◽  
Grigory L. Dianov
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Base Excision

scholarly journals A novel regulatory circuit in base excision repair involving AP endonuclease 1, Creb1 and DNA polymerase β

2010 ◽  
Vol 39 (8) ◽  
pp. 3156-3165 ◽  
Author(s):  
De-Sheng Pei ◽  
Xiao-Jie Yang ◽  
Wei Liu ◽  
Jeroen E. J. Guikema ◽  
Carol E. Schrader ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Ap Endonuclease ◽  
Regulatory Circuit ◽  
Ap Endonuclease 1 ◽  
Base Excision

scholarly journals Dynamic Compartmentalization of Base Excision Repair Proteins in Response to Nuclear and Mitochondrial Oxidative Stress

2008 ◽  
Vol 29 (3) ◽  
pp. 794-807 ◽  
Author(s):  
Lyra M. Griffiths ◽  
Dan Swartzlander ◽  
Kellen L. Meadows ◽  
Keith D. Wilkinson ◽  
Anita H. Corbett ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Dna Damage ◽  
Dna Repair ◽  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Intracellular Localization ◽  
Genotoxic Stress ◽  
Mitochondrial Oxidative Stress ◽  
Base Excision

ABSTRACT DNAs harbored in both nuclei and mitochondria of eukaryotic cells are subject to continuous oxidative damage resulting from normal metabolic activities or environmental insults. Oxidative DNA damage is primarily reversed by the base excision repair (BER) pathway, initiated by N-glycosylase apurinic/apyrimidinic (AP) lyase proteins. To execute an appropriate repair response, BER components must be distributed to accommodate levels of genotoxic stress that may vary considerably between nuclei and mitochondria, depending on the growth state and stress environment of the cell. Numerous examples exist where cells respond to signals, resulting in relocalization of proteins involved in key biological transactions. To address whether such dynamic localization contributes to efficient organelle-specific DNA repair, we determined the intracellular localization of the Saccharomyces cerevisiae N-glycosylase/AP lyases, Ntg1 and Ntg2, in response to nuclear and mitochondrial oxidative stress. Fluorescence microscopy revealed that Ntg1 is differentially localized to nuclei and mitochondria, likely in response to the oxidative DNA damage status of the organelle. Sumoylation is associated with targeting of Ntg1 to nuclei containing oxidative DNA damage. These studies demonstrate that trafficking of DNA repair proteins to organelles containing high levels of oxidative DNA damage may be a central point for regulating BER in response to oxidative stress.

scholarly journals Base excision repair of oxidative DNA damage and association with cancer and aging

2008 ◽  
Vol 30 (1) ◽  
pp. 2-10 ◽  
Author(s):  
S. Maynard ◽  
S. H. Schurman ◽  
C. Harboe ◽  
N. C. de Souza-Pinto ◽  
V. A. Bohr
Keyword(s):  
Dna Damage ◽  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Base Excision

scholarly journals Protection against Methylation-induced Cytotoxicity by DNA Polymerase β-Dependent Long Patch Base Excision Repair

2000 ◽  
Vol 275 (3) ◽  
pp. 2211-2218 ◽  
Author(s):  
Julie K. Horton ◽  
Rajendra Prasad ◽  
Esther Hou ◽  
Samuel H. Wilson
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Base Excision

scholarly journals The Effect ofMsh2Knockdown on Toxicity Induced bytert-Butyl-hydroperoxide, Potassium Bromate, and Hydrogen Peroxide in Base Excision Repair Proficient and Deficient Cells

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
N. Cooley ◽  
R. H. Elder ◽  
A. C. Povey
Keyword(s):  
Dna Damage ◽  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Shrna Expression ◽  
Cellular Toxicity ◽  
Dna Mismatch ◽  
Shrna Expression Vector ◽  
Repair Systems ◽  
Base Excision

The DNA mismatch repair (MMR) and base excision repair (BER) systems are important determinants of cellular toxicity following exposure to agents that cause oxidative DNA damage. To examine the interactions between these different repair systems, we examined whether toxicity, induced byt-BOOH and KBrO3, differs in BER proficient (Mpg+/+,Nth1+/+) and deficient (Mpg−/−,Nth1−/−) mouse embryonic fibroblasts (MEFs) followingMsh2knockdown of between 79 and 88% using an shRNA expression vector.Msh2knockdown inNth1+/+cells had no effect ont-BOOH and KBrO3induced toxicity as assessed by an MTT assay; knockdown inNth1−/−cells resulted in increased resistance tot-BOOH and KBrO3, a result consistent with Nth1 removing oxidised pyrimidines.Msh2knockdown inMpg+/+cells had no effect ont-BOOH toxicity but increased resistance to KBrO3; inMpg−/−cells,Msh2knockdown increased cellular sensitivity to KBrO3but increased resistance to t-BOOH, suggesting a role forMpgin removing DNA damage induced by these agents. MSH2 dependent and independent pathways then determine cellular toxicity induced by oxidising agents. A complex interaction between MMR and BER repair systems, that is, exposure dependent, also exists to determine cellular toxicity.

scholarly journals Apurinic/Apyrimidinic Endonuclease (APE/REF-1) Haploinsufficient Mice Display Tissue-specific Differences in DNA Polymerase β-Dependent Base Excision Repair

2004 ◽  
Vol 279 (18) ◽  
pp. 18425-18433 ◽  
Author(s):  
Julian J. Raffoul ◽  
Diane C. Cabelof ◽  
Jun Nakamura ◽  
Lisiane B. Meira ◽  
Errol C. Friedberg ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Tissue Specific ◽  
Base Excision
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