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A Novel G-Quadruplex Binding Protein in Yeast-Slx9
Silvia Götz1,2, Satyaprakash Pandey1,3, Sabrina Bartsch2
1University of Groningen, University Medical Center Groningen, European Research Institute for the Biology of Ageing, 9713 AV Groningen, The Netherlands. goetzsilvia@yahoo.de.
Molecules (Basel, Switzerland)
|May 10, 2019
Summary
Slx9 protein binds G-quadruplex (G4) DNA structures. Its binding increases when Sgs1 helicase is absent, suggesting Slx9 protects stabilized G4 structures in yeast.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- G-quadruplex (G4) structures are stable DNA/RNA secondary structures crucial for biological processes.
- Specific proteins are required for G4 formation and unwinding due to their high stability.
Purpose of the Study:
- To identify novel G4-binding proteins.
- To investigate the in vivo role of Slx9 in G4 structure regulation.
Main Methods:
- Yeast one-hybrid screen to identify G4-binding proteins.
- In vitro binding assays to confirm protein-G4 interaction.
- Genome-wide ChIP-seq analysis in Saccharomyces cerevisiae.
- Genetic analyses involving Sgs1 helicase.
Main Results:
- Slx9 was identified as a novel G4 DNA-binding protein.
- Slx9 binds G4 DNA structures in vitro.
- Genome-wide binding of Slx9 to G4 regions is low in wild-type yeast.
- Slx9 binding significantly increases in the absence of the Sgs1 helicase.
Conclusions:
- Slx9 recognizes and binds to G4 DNA structures.
- Slx9 plays a role in protecting stabilized G4 structures in vivo.
- The function of Slx9 in G4 regulation is dependent on the presence of Sgs1 helicase.
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