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Updated: Jul 20, 2026
10:39
A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae
Published on: September 17, 2020
Rev1 enhances CAG.CTG repeat stability in Saccharomyces cerevisiae
Natasha S Collins1, Saumitri Bhattacharyya, Robert S Lahue
1Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Box 986805, Omaha, NE 68198-6805, United States.
DNA Repair
|September 19, 2006
Summary
Yeast Rev1 protein unexpectedly protects against trinucleotide repeat expansions, a key factor in genetic diseases. This function relies on its BRCT domain, not DNA polymerase zeta.
Area of Science:
- Genetics
- Molecular Biology
- Genomic Instability
Background:
- Trinucleotide repeats (TNRs) are prone to expansion, causing genetic diseases.
- DNA replication and repair are implicated in TNR instability.
- Proteins modulating TNR mutability are crucial for understanding disease pathogenesis.
Purpose of the Study:
- To identify novel proteins that protect cells against TNR instability.
- To investigate the role of the yeast Rev1 protein in TNR dynamics.
Main Methods:
- Isolation and characterization of yeast mutants exhibiting increased CAG.CTG tract expansions.
- Analysis of Rev1's effect on TNR expansion and contraction rates.
- Assessment of Rev1's function in relation to its BRCT domain and dCMP transferase activity, and its interaction with DNA polymerase zeta subunits (REV3, REV7).
Main Results:
- A rev1 mutant showed increased rates of CAG.CTG repeat expansions and contractions, indicating Rev1 normally inhibits TNR instability.
- Rev1's protective effect was specific to TNRs capable of forming hairpins.
- Rev1's function in TNR stability was dependent on its BRCT domain but independent of its dCMP transferase activity and DNA polymerase zeta.
Conclusions:
- Yeast Rev1 acts as a suppressor of trinucleotide repeat instability.
- Rev1's role in maintaining genome stability at TNRs is mediated through its BRCT domain.
- These findings reveal a novel mechanism for controlling TNR expansions, independent of DNA polymerase zeta.
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