scholarly journals Weak Strand Displacement Activity Enables Human DNA Polymerase β to Expand CAG/CTG Triplet Repeats at Strand Breaks

2002 ◽  
Vol 277 (44) ◽  
pp. 41379-41389 ◽  
Author(s):  
Michael J. Hartenstine ◽  
Myron F. Goodman ◽  
John Petruska
Keyword(s):  
Dna Polymerase ◽  
Strand Displacement ◽  
Triplet Repeats ◽  
Dna Polymerase Β ◽  
Strand Breaks ◽  
Displacement Activity ◽  
Human Dna

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

Detection and characterization of DNA polymerase activity in Toxoplasma gondii

Parasitology ◽  
1993 ◽  
Vol 107 (2) ◽  
pp. 135-139 ◽  
Author(s):  
A. Makioka ◽  
B. Stavros ◽  
J. T. Ellis ◽  
A. M. Johnson
Keyword(s):  
Toxoplasma Gondii ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Sedimentation Coefficient ◽  
Polymerase Activity ◽  
Magnesium Ions ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Approximate Molecular Weight

SUMMARYA DNA polymerase activity has been detected and characterized in crude extracts from tachzoites of Toxoplasma gondii. The enzyme has a sedimentation coefficient of 6·4 S, corresponding to an approximate molecular weight of 150000 assuming a globular shape. Like mammalian DNA polymerase α, the DNA polymerase of T. gondii was sensitive to N-ethylmaleimide and inhibited by high ionic strength. However, the enzyme activity was not inhibited by aphidicolin which is an inhibitor of mammalian DNA polymerases α, δ and ε and also cytosine-β-D-arabinofuranoside-5′-triphosphate which is an inhibitor of α polymerase. The activity was inhibited by 2′,3′-dideoxythymidine-5′-triphosphate which is an inhibitor of mammalian DNA polymerase β and γ. Magnesium ions (Mg2+) were absolutely required for activity and its optimal concentration was 6 mM. The optimum potassium (K+) concentration was 50 mM and a higher concentration of K+ markedly inhibited the activity. Activity was optimal at pH 8. Monoclonal antibodies against human DNA polymerase did not bind to DNA polymerase of T. gondii. Thus the T. gondii enzyme differs from the human enzymes and may be a useful target for the design of toxoplasmacidal drugs.

scholarly journals Thermodynamics of Human DNA Ligase I Trimerization and Association with DNA Polymerase β

1998 ◽  
Vol 273 (32) ◽  
pp. 20540-20550 ◽  
Author(s):  
Emilios K. Dimitriadis ◽  
Rajendra Prasad ◽  
Mary K. Vaske ◽  
Ling Chen ◽  
Alan E. Tomkinson ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Dna Ligase I

scholarly journals A Facile Semisynthesis and Evaluation of Garcinoic Acid and Its Analogs for the Inhibition of Human DNA Polymerase β

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5847
Author(s):  
Satheesh Gujarathi ◽  
Maroof Khan Zafar ◽  
Xingui Liu ◽  
Robert L. Eoff ◽  
Guangrong Zheng
Keyword(s):  
Natural Product ◽  
Dna Polymerase ◽  
Activity Relationship ◽  
Synthetic Method ◽  
Valuable Insight ◽  
Dna Polymerase Β ◽  
Sar Studies ◽  
Human Dna ◽  
Structure Activity ◽  
Insight Into

Garcinoic acid has been identified as an inhibitor of DNA polymerase β (pol β). However, no structure-activity relationship (SAR) studies of garcinoic acid as a pol β inhibitor have been conducted, in part due to the lack of an efficient synthetic method for this natural product and its analogs. We developed an efficient semi-synthetic method for garcinoic acid and its analogs by starting from natural product δ-tocotrienol. Our preliminary SAR studies provided a valuable insight into future discovery of garcinoic acid-based pol β inhibitors.

scholarly journals Strand Displacement Activity of PrimPol

2020 ◽  
Vol 21 (23) ◽  
pp. 9027
Author(s):  
Elizaveta O. Boldinova ◽  
Ekaterina A. Belousova ◽  
Diana I. Gagarinskaya ◽  
Ekaterina A. Maltseva ◽  
Svetlana N. Khodyreva ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Strand Displacement ◽  
Displacement Activity

Human PrimPol is a unique enzyme possessing DNA/RNA primase and DNA polymerase activities. In this work, we demonstrated that PrimPol efficiently fills a 5-nt gap and possesses the conditional strand displacement activity stimulated by Mn2+ ions and accessory replicative proteins RPA and PolDIP2. The DNA displacement activity of PrimPol was found to be more efficient than the RNA displacement activity and FEN1 processed the 5′-DNA flaps generated by PrimPol in vitro.

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