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Purification of the Dynamin-Related Protein Vps1 Using Mammalian and Bacterial Expression Systems
Natalia V Varlakhanova1, Marijn G J Ford2
1Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Methods in Molecular Biology (Clifton, N.J.)
|June 13, 2020
Summary
This study details purification protocols for Chaetomium thermophilum Vps1, a model fungal dynamin-related protein (DRP). These methods enable the study of DRPs essential for cellular trafficking and homeostasis.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- Dynamin-related proteins (DRPs) are crucial for cellular membrane remodeling.
- DRPs play vital roles in fundamental cellular trafficking and homeostasis.
- Understanding DRP structure and function requires efficient purification methods.
Purpose of the Study:
- To describe laboratory protocols for purifying Chaetomium thermophilum Vps1.
- To enable the study of a model fungal DRP.
- To provide methods for purifying both full-length and minimal DRP constructs.
Main Methods:
- Utilized mammalian expression systems for protein production.
- Employed Escherichia coli expression systems for protein production.
- Developed protocols for the purification of full-length and minimal constructs of CtVps1.
Main Results:
- Successfully purified full-length Chaetomium thermophilum Vps1.
- Successfully purified minimal constructs of Chaetomium thermophilum Vps1.
- Established robust protocols applicable to both expression systems.
Conclusions:
- The described protocols facilitate the purification of the fungal DRP, CtVps1.
- These methods are essential for further investigation into DRP function.
- The purification of CtVps1 provides a foundation for studying DRPs in cellular processes.
