Related Experiment Video
Updated: May 22, 2026

07:38
DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis
Published on: October 6, 2017
DNA polymerase beta (pol β) inhibitors: a comprehensive overview
Khaled H Barakat1, Melissa M Gajewski, Jack A Tuszynski
1Department of Physics, University of Alberta, Edmonton, AB, Canada. kbarakat@ualberta.ca
Drug Discovery Today
|May 8, 2012
Summary
Base excision repair (BER) eliminates damaged DNA bases. DNA polymerase beta (pol β) is crucial for BER but current inhibitors lack potency and specificity for drug development.
Area of Science:
- Molecular Biology
- Biochemistry
- Pharmacology
Background:
- Base excision repair (BER) is a critical DNA repair pathway.
- DNA polymerase beta (pol β) is an essential enzyme in BER.
- Pol β is a potential therapeutic target for various diseases.
Purpose of the Study:
- To compile a knowledge base on DNA polymerase beta (pol β) inhibitors.
- To review structures, inhibition modes, and activities of pol β inhibitors.
- To assess the pharmacological potential of existing pol β inhibitors.
Main Methods:
- Literature review of identified pol β inhibitors.
- Analysis of structural data for pol β inhibitors.
- Evaluation of inhibition mechanisms and enzymatic activities.
- Assessment of inhibitor potency and specificity.
Main Results:
- Over 60 pol β inhibitors have been identified.
- Many existing inhibitors lack sufficient potency or specificity.
- Significant structural diversity exists among pol β inhibitors.
- Varied modes of inhibition have been observed.
Conclusions:
- DNA polymerase beta (pol β) remains a promising therapeutic target.
- Development of potent and specific pol β inhibitors is challenging.
- Further research is needed to optimize pol β inhibitors for drug development.
- Understanding inhibitor structures and activities is key to advancing BER-targeted therapies.
More Related Videos
Related Concept Videos
Inhibitors of Bacterial DNA Synthesis
Bacterial pathogens depend on precise and efficient DNA replication to sustain infection. Two type II topoisomerases—DNA gyrase and topoisomerase IV—are critical to this process, as they resolve DNA supercoiling and unlink chromosomes during replication. Fluoroquinolones, synthetic derivatives of quinolones, exploit this mechanism by stabilizing the transient DNA–enzyme cleavage complex, preventing strand religation, and causing lethal double-strand breaks. These antibiotics are selectively...
Inhibitors of Viral Protein Synthesis
Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Proofreading
Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore, it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase Enzyme
Errors During Replication are Corrected by the DNA Polymerase Enzyme
Proofreading
Overview
Translesion DNA Polymerases
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
Bacterial RNA Polymerase
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...

