Visualizing Protein Interactions in Yeast Cells
Author Information
Author(s): Akman Gökhan, MacNeill Stuart A
Primary Institution: Department of Biology, University of Copenhagen
Hypothesis
Can bimolecular fluorescence complementation (BiFC) be used to visualize interactions between components of the CMG complex in fission yeast?
Conclusion
BiFC can effectively visualize interactions between GINS and MCM complexes in fission yeast cells during S-phase.
Supporting Evidence
- BiFC was applied for the first time in fission yeast to study protein interactions.
- Interactions between GINS and MCM were visualized in the nuclei of exponentially-growing cells.
- MCM-MCM interactions were also observed on chromatin in S-phase cells.
Takeaway
The study shows how scientists can use a special technique to see how proteins interact in yeast cells, which helps us understand DNA replication better.
Methodology
Bimolecular fluorescence complementation (BiFC) was used to analyze protein-protein interactions in fission yeast.
Limitations
The tight binding of YFP fragments may interfere with the normal dynamics of protein interactions, potentially leading to experimental artifacts.
Digital Object Identifier (DOI)
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