Expressing Tung Tree DGAT1 in E. coli
Author Information
Author(s): Heping Cao, Dorselyn Chapital, Jay Shockey, K Thomas Klasson
Primary Institution: Commodity Utilization Research Unit, Southern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture
Hypothesis
The objective of this study was to establish a procedure for expressing full-length DGAT1 in E. coli.
Conclusion
This study reports the first procedure for expressing full-length DGAT1 from any species using a bacterial expression system.
Supporting Evidence
- The study successfully expressed a full-length DGAT1 protein in E. coli for the first time.
- Recombinant DGAT1 was found to be extensively degraded and associated with other proteins and membranes.
- Multiple proteins co-purified with the DGAT1 fusion protein during purification.
Takeaway
The researchers figured out how to make a specific protein from a tung tree in bacteria, which is usually hard to do. This could help scientists learn more about how this protein works.
Methodology
The study involved constructing an expression plasmid for DGAT1, transforming it into E. coli, and using various purification techniques.
Limitations
The protein was not purified to homogeneity, and extensive degradation of the recombinant protein was observed.
Digital Object Identifier (DOI)
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