scholarly journals Single-nucleotide base excision repair DNA polymerase activity in C. elegans in the absence of DNA polymerase  

2011 ◽  
Vol 40 (2) ◽  
pp. 670-681 ◽  
Author(s):  
K. Asagoshi ◽  
W. Lehmann ◽  
E. K. Braithwaite ◽  
L. Santana-Santos ◽  
R. Prasad ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Polymerase Activity ◽  
Single Nucleotide ◽  
C Elegans ◽  
Nucleotide Base ◽  
Base Excision

scholarly journals Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β

2007 ◽  
Vol 282 (18) ◽  
pp. 13532-13541 ◽  
Author(s):  
Yuan Liu ◽  
Rajendra Prasad ◽  
William A. Beard ◽  
Padmini S. Kedar ◽  
Esther W. Hou ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Single Nucleotide ◽  
Nucleotide Base ◽  
Base Excision

scholarly journals The Base Substitution Fidelity of DNA Polymerase β-dependent Single Nucleotide Base Excision Repair

2003 ◽  
Vol 278 (28) ◽  
pp. 25947-25951 ◽  
Author(s):  
Toshiro Matsuda ◽  
Brian J. Vande Berg ◽  
Katarzyna Bebenek ◽  
Wendy P. Osheroff ◽  
Samuel H. Wilson ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Base Substitution ◽  
Dna Polymerase Β ◽  
Single Nucleotide ◽  
Nucleotide Base ◽  
Base Excision

scholarly journals Human DNA polymerase   possesses 5'-dRP lyase activity and functions in single-nucleotide base excision repair in vitro

2009 ◽  
Vol 37 (6) ◽  
pp. 1868-1877 ◽  
Author(s):  
R. Prasad ◽  
M. J. Longley ◽  
F. S. Sharief ◽  
E. W. Hou ◽  
W. C. Copeland ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Single Nucleotide ◽  
Nucleotide Base ◽  
Human Dna ◽  
Lyase Activity ◽  
Base Excision

scholarly journals The Base Excision Repair Pathway in the Nematode Caenorhabditis elegans

2020 ◽  
Vol 8 ◽  
Author(s):  
Noha Elsakrmy ◽  
Qiu-Mei Zhang-Akiyama ◽  
Dindial Ramotar
Keyword(s):  
Dna Repair ◽  
Caenorhabditis Elegans ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylases ◽  
Repair Synthesis ◽  
C Elegans ◽  
Base Excision ◽  
Dna Repair Synthesis

Exogenous and endogenous damage to the DNA is inevitable. Several DNA repair pathways including base excision, nucleotide excision, mismatch, homologous and non-homologous recombinations are conserved across all organisms to faithfully maintain the integrity of the genome. The base excision repair (BER) pathway functions to repair single-base DNA lesions and during the process creates the premutagenic apurinic/apyrimidinic (AP) sites. In this review, we discuss the components of the BER pathway in the nematode Caenorhabditis elegans and delineate the different phenotypes caused by the deletion or the knockdown of the respective DNA repair gene, as well as the implications. To date, two DNA glycosylases have been identified in C. elegans, the monofunctional uracil DNA glycosylase-1 (UNG-1) and the bifunctional endonuclease III-1 (NTH-1) with associated AP lyase activity. In addition, the animal possesses two AP endonucleases belonging to the exonuclease-3 and endonuclease IV families and in C. elegans these enzymes are called EXO-3 and APN-1, respectively. In mammalian cells, the DNA polymerase, Pol beta, that is required to reinsert the correct bases for DNA repair synthesis is not found in the genome of C. elegans and the evidence indicates that this role could be substituted by DNA polymerase theta (POLQ), which is known to perform a function in the microhomology-mediated end-joining pathway in human cells. The phenotypes observed by the C. elegans mutant strains of the BER pathway raised many challenging questions including the possibility that the DNA glycosylases may have broader functional roles, as discuss in this review.

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
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