Characterization of Dad1p in the Dam1-DASH Complex
Author Information
Author(s): Jennifer Waldo, Michael Scherrer
Primary Institution: Department of Biology, SUNY New Paltz, New Paltz, New York, United States of America
Hypothesis
Can Dad1p be effectively expressed and characterized as a component of the Dam1-DASH kinetochore complex?
Conclusion
The study successfully produced and characterized Dad1p, revealing its potential role in oligomerization within the Dam1-DASH complex.
Supporting Evidence
- Dad1p was successfully expressed in E. coli and purified to >95% purity.
- The study demonstrated that Dad1p can form dimers and/or tetramers depending on concentration.
- The research provides a new tool for studying the Dam1-DASH complex.
Takeaway
The researchers figured out how to make a protein called Dad1p that helps cells divide, which could help us understand how cells work better.
Methodology
The study involved cloning the DAD1 gene, expressing it in E. coli, and purifying the Dad1p protein using various chromatography techniques.
Limitations
The individual Dam1-DASH subunits are not soluble when expressed in E. coli, which limits the types of experiments that can be conducted.
Digital Object Identifier (DOI)
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