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 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 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 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 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

scholarly journals MSH2–MSH6 stimulates DNA polymerase η, suggesting a role for A:T mutations in antibody genes

2005 ◽  
Vol 201 (4) ◽  
pp. 637-645 ◽  
Author(s):  
Teresa M. Wilson ◽  
Alexandra Vaisman ◽  
Stella A. Martomo ◽  
Patsa Sullivan ◽  
Li Lan ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Somatic Hypermutation ◽  
Excision Repair ◽  
Cytidine Deaminase ◽  
Abasic Site ◽  
Cell Extracts ◽  
Activation Induced Cytidine Deaminase ◽  
Base Excision

Activation-induced cytidine deaminase deaminates cytosine to uracil (dU) in DNA, which leads to mutations at C:G basepairs in immunoglobulin genes during somatic hypermutation. The mechanism that generates mutations at A:T basepairs, however, remains unclear. It appears to require the MSH2–MSH6 mismatch repair heterodimer and DNA polymerase (pol) η, as mutations of A:T are decreased in mice and humans lacking these proteins. Here, we demonstrate that these proteins interact physically and functionally. First, we show that MSH2–MSH6 binds to a U:G mismatch but not to other DNA intermediates produced during base excision repair of dUs, including an abasic site and a deoxyribose phosphate group. Second, MSH2 binds to pol η in solution, and endogenous MSH2 associates with the pol in cell extracts. Third, MSH2–MSH6 stimulates the catalytic activity of pol η in vitro. These observations suggest that the interaction between MSH2–MSH6 and DNA pol η stimulates synthesis of mutations at bases located downstream of the initial dU lesion, including A:T pairs.

scholarly journals DNA polymerase X from Deinococcus radiodurans implicated in bacterial tolerance to DNA damage is characterized as a short patch base excision repair polymerase

Microbiology ◽  
2009 ◽  
Vol 155 (9) ◽  
pp. 3005-3014 ◽  
Author(s):  
Nivedita P. Khairnar ◽  
Hari S. Misra
Keyword(s):  
Dna Damage ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Deinococcus Radiodurans ◽  
Excision Repair ◽  
Strand Break ◽  
Klenow Fragment ◽  
E Coli ◽  
Base Excision

The Deinococcus radiodurans R1 genome encodes an X-family DNA repair polymerase homologous to eukaryotic DNA polymerase β. The recombinant deinococcal polymerase X (PolX) purified from transgenic Escherichia coli showed deoxynucleotidyltransferase activity. Unlike the Klenow fragment of E. coli, this enzyme showed short patch DNA synthesis activity on heteropolymeric DNA substrate. The recombinant enzyme showed 5′-deoxyribose phosphate (5′-dRP) lyase activity and base excision repair function in vitro, with the help of externally supplied glycosylase and AP endonuclease functions. A polX disruption mutant of D. radiodurans expressing 5′-dRP lyase and a truncated polymerase domain was comparatively less sensitive to γ-radiation than a polX deletion mutant. Both mutants showed higher sensitivity to hydrogen peroxide. Excision repair mutants of E. coli expressing this polymerase showed functional complementation of UV sensitivity. These results suggest the involvement of deinococcal polymerase X in DNA-damage tolerance of D. radiodurans, possibly by contributing to DNA double-strand break repair and base excision repair.

Human DNA polymerase λ catalyzes lesion bypass across benzo[a]pyrene-derived DNA adduct during base excision repair

DNA Repair ◽  
2012 ◽  
Vol 11 (4) ◽  
pp. 367-373 ◽  
Author(s):  
Lidia V. Skosareva ◽  
Natalia A. Lebedeva ◽  
Nadejda I. Rechkunova ◽  
Alexander Kolbanovskiy ◽  
Nicholas E. Geacintov ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Adduct ◽  
Lesion Bypass ◽  
Human Dna ◽  
Dna Polymerase Λ ◽  
Base Excision
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