ArticleApplied microbiology and biotechnology2016
A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae.
Article in Applied microbiology and biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Dual-channel optogenetics in yeast for multiplexed light-based control of cellular processes and pathways.Nature communications · 2026Article
- Functional expression of recombinant insulins in Saccharomyces cerevisiae.Microbial cell factories · 2024Article
- Engineering strategies for enhanced heterologous protein production by Saccharomyces cerevisiae.Microbial cell factories · 2024Review
- Modulation of Kex2p Cleavage Site for In Vitro Processing of Recombinant Proteins Produced byJournal of microbiology and biotechnology · 2023Article
- Development of a Novel ATP Bioluminescence Assay Based on Engineered ProbioticJournal of microbiology and biotechnology · 2023Article
- A new platform host for strong expression underBiotechnology reports (Amsterdam, Netherlands) · 2022Article
- Production of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins.Applied microbiology and biotechnology · 2022Article
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
- Review
- Secretome-based screening of fusion partners and their application in recombinant protein secretion in Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2022Article
- Directed evolution and secretory expression of xylose isomerase for improved utilisation of xylose in Saccharomyces cerevisiae.Biotechnology for biofuels · 2021Article
- A study on the use of strain-specific and homologous promoters for heterologous expression in industrial Saccharomyces cerevisiae strains.AMB Express · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The VOA1 (YGR106C) gene of Saccharomyces cerevisiae encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography.
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