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Identification of protein complexes with quantitative proteomics in S. cerevisiae
Published on: March 4, 2009
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Expression of recombinant multi-protein complexes in Saccharomyces cerevisiae
1Laboratory of DNA Replication, The Rockefeller University, New York, NY, United States.
Methods in Enzymology
|November 7, 2021
Summary
Baker's yeast, Saccharomyces cerevisiae, offers a simple, cost-effective method for producing complex eukaryotic proteins. This system facilitates eukaryotic post-translational modifications and co-expression of multiple genes for multi-protein complexes.
Area of Science:
- Biotechnology
- Molecular Biology
- Biochemistry
Background:
- Baker's yeast (Saccharomyces cerevisiae) is a widely used microbial host for recombinant protein expression.
- Bacterial expression systems lack eukaryotic post-translational modification capabilities.
- Producing large, multi-protein complexes often requires co-expression of multiple genes.
Purpose of the Study:
- To provide protocols for inducible expression of recombinant genes in Saccharomyces cerevisiae.
- To detail methods for integrating recombinant genes into yeast chromosomes for stable expression.
- To enable efficient production of eukaryotic proteins and multi-protein complexes.
Main Methods:
- Utilizing episomal plasmid vectors for inducible gene expression.
- Integrating recombinant genes into yeast chromosomes for stable expression.
- Employing rich media for rapid growth and induction of expression cells.
Main Results:
- Demonstrated successful inducible expression of recombinant eukaryotic proteins.
- Showcased the ability to co-express multiple genes for complex formation.
- Established protocols for both episomal and chromosomal integration strategies.
Conclusions:
- Saccharomyces cerevisiae is a powerful and accessible system for recombinant protein production.
- The provided protocols facilitate efficient expression and modification of eukaryotic proteins.
- Yeast expression systems are advantageous for producing complex, modified proteins and multi-protein complexes.
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