ArticleMicrobial biotechnology2022
Avoiding entry into intracellular protein degradation pathways by signal mutations increases protein secretion in Pichia pastoris.
Article in Microbial biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 24 citations in OpenAlex.
- Systematic optimization ofEngineering microbiology · 2026Review
- High-efficiency secretion expression of FAD-dependent glucose dehydrogenase in Pichia pastoris via signal peptide optimization and redox cofactor enhancement.Bioprocess and biosystems engineering · 2026Article
- Production of Recombinant Hemoglobin inFoods (Basel, Switzerland) · 2026Article
- Advances in Key Genetic Elements and Strategies for High-Yield Heterologous Protein Expression inJournal of fungi (Basel, Switzerland) · 2026Review
- Recombinant Expression of Chitinase CtChi70 in Komagataella phaffii for Sustainable N, N'-Diacetyl-Chitobiose Production From Shrimp Shells.Biotechnology journal · 2026Article
- Efficient Expression of Lactone Hydrolase Cr2zen for Scalable Zearalenone Degradation inToxins · 2025Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- A toolkit for facilitating markerless integration of expression cassettes in Komagataella phaffii via CRISPR/Cas9.Microbial cell factories · 2025Article
- Designing strong inducible synthetic promoters in yeasts.Nature communications · 2024Article
- A Cost-EffectiveBioengineering (Basel, Switzerland) · 2024Article
- Advances in Metabolic Engineering ofJournal of fungi (Basel, Switzerland) · 2023Review
- Avoiding entry into intracellular protein degradation pathways by signal mutations increases protein secretion in Pichia pastoris.Microbial biotechnology · 2022Article
- A streamlined strain engineering workflow with genome-wide screening detects enhanced protein secretion in Komagataella phaffii.Communications biology · 2022Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In our previous study, we serendipitously discovered that protein secretion in the methylotrophic yeast Pichia pastoris is enhanced by a mutation (V50A) in the mating factor alpha (MFα) prepro-leader signal derived from Saccharomyces cerevisiae. In the present study, we investigated 20 single-amino-acid substitutions, including V50A, located within the MFα signal peptide, indicating that V50A and several single mutations alone provided significant increase in production of the secreted proteins. In addition to hydrophobicity index analysis, both an unfolded protein response (UPR) biosensor analysis and a microscopic observation showed a clear difference on the levels of UPR induction and mis-sorting of secretory protein into vacuoles among the wild-type and mutated MFα signal peptides. This work demonstrates the importance of avoiding entry of secretory proteins into the intracellular protein degradation pathways, an observation that is expected to contribute to the engineering of strains with increased production of recombinant secreted proteins.
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