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Updated: Feb 6, 2026

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
Published on: April 4, 2025
The deoxyribose phosphate lyase of DNA polymerase β suppresses a processive DNA synthesis to prevent trinucleotide
Yanhao Lai1, Yossi Weizmann2, Yuan Liu1,3,4
1Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th Street, Miami, FL 33199, USA.
Abstract:
Trinucleotide repeat (TNR) instability is associated with over 42 neurodegenerative diseases and cancer, for which the molecular mechanisms remain to be elucidated. We have shown that the DNA base excision repair (BER) pathway and its central component, DNA polymerase β (pol β), in particular, its polymerase activity plays an active role in regulating somatic TNR instability. Herein, we revealed a unique role of the pol β dRP lyase in preventing somatic TNR instability. We found that deficiency of pol β deoxyribose phosphate (dRP) lyase activity locked the pol β dRP lyase domain to a dRP group, and this 'tethered' pol β to its template forcing the polymerase to perform a processive DNA synthesis. This subsequently promoted DNA strand slippage allowing pol β to skip over a template loop and causing TNR deletion. We showed that the effects were eliminated by complementation of the dRP lyase deficiency with wild-type pol β protein. The results indicate that pol β dRP lyase activity restrained the pol β-dRP interaction to suppress a pol β processive DNA synthesis, thereby preventing TNR deletion. This further implicates a potential of pol β dRP lyase inhibition as a novel treatment of TNR-expansion diseases.
Insights
DNA polymerase β's dRP lyase activity prevents trinucleotide repeat (TNR) instability by stopping processive DNA synthesis. Inhibiting this activity may offer new treatments for TNR-expansion diseases.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Trinucleotide repeat (TNR) instability is implicated in over 42 neurodegenerative diseases and cancers.
- The precise molecular mechanisms driving TNR instability are not fully understood.
- The DNA base excision repair (BER) pathway, particularly DNA polymerase β (pol β), is known to regulate somatic TNR instability.
Purpose of the Study:
- To investigate the specific role of the pol β dRP lyase domain in preventing somatic TNR instability.
- To elucidate the molecular mechanism by which pol β dRP lyase activity impacts TNR stability.
Main Methods:
- Investigating the effects of pol β dRP lyase deficiency on TNR instability in cellular models.
- Analyzing the interaction between pol β and its DNA template in the presence and absence of functional dRP lyase activity.
- Assessing the impact of wild-type pol β complementation on TNR instability in deficient cells.
Main Results:
- Deficiency in pol β dRP lyase activity leads to 'tethering' of pol β to the DNA template, promoting processive DNA synthesis.
- This processive synthesis results in DNA strand slippage and trinucleotide repeat deletion.
- Complementation with wild-type pol β protein restored normal TNR stability, eliminating deletions.
Conclusions:
- Pol β dRP lyase activity is crucial for restraining pol β-template interactions, thereby suppressing processive DNA synthesis and preventing TNR deletion.
- The findings suggest that pol β dRP lyase inhibition could be a potential therapeutic strategy for TNR-expansion diseases.
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