ArticleMicrobial biotechnology2019
New tools for high-throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris.
Article in Microbial biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Effect ofMolecules (Basel, Switzerland) · 2023Article
- An outlook to sophisticated technologies and novel developments for metabolic regulation in theFrontiers in bioengineering and biotechnology · 2023Review
- Article
- Harnessing the Endogenous 2μ Plasmid ofFrontiers in microbiology · 2021Article
- New tools for high-throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris.Microbial biotechnology · 2019Article
- Recent Developments in Bioprocessing of Recombinant Proteins: Expression Hosts and Process Development.Frontiers in bioengineering and biotechnology · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterologous protein expression in yeast, mostly in Saccharomyces cerevisiae and Pichia pastoris, is a well-established and widely used technique. It typically requires the construction of an expression vector in Escherichia coli containing the foreign gene and its subsequent transformation into yeast. Although simple, this procedure has important limitations for the expression of large numbers of proteins, that is, for the generation of protein libraries. We describe here the development of a novel system for the easy and fast expression of heterologous proteins both in S. cerevisiae and in P. pastoris, under the control of the GAL1 and AOX1 promoters respectively. Expression in S. cerevisiae requires only the transformation of yeast cells with an unpurified PCR product carrying the gene to be expressed, and the expression of the same gene in P. pastoris requires only the isolation of the plasmid generated in S. cerevisiae and its transformation into this second yeast, thus making this system suitable for high-throughput projects. The system has been tested by the extracellular expression of 30 secretory fungal proteins.
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Registered trials
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