ArticleApplied and environmental microbiology2005
Reduced proteolysis of secreted gelatin and Yps1-mediated alpha-factor leader processing in a Pichia pastoris kex2 disruptant.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 55 citations in OpenAlex.
- Engineering Saccharomyces cerevisiae secretory system for recombinant protein production: strategies from signal peptides to protease control.Archives of microbiology · 2026Review
- Characterizing the role of an endogenous serine protease KpSub2 in recombinant collagen degradation in Komagataella phaffii.Bioresources and bioprocessing · 2026Article
- Expression and purification of a broad-spectrum human protease inhibitor inBiochemistry and biophysics reports · 2025Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- Strains and Molecular Tools for Recombinant Protein Production in Pichia pastoris.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Customized yeast cell factories for biopharmaceuticals: from cell engineering to process scale up.Microbial cell factories · 2021Review
- Challenging the workhorse: Comparative analysis of eukaryotic micro-organisms for expressing monoclonal antibodies.Biotechnology and bioengineering · 2019Article
- Nanofibrillar hydrogel scaffolds from recombinant protein-based polymers with integrin- and proteoglycan-binding domains.Journal of biomedical materials research. Part A · 2016Article
- Cloning and expression of synthetic genes encoding the broad antimicrobial spectrum bacteriocins SRCAM 602, OR-7, E-760, and L-1077, by recombinant Pichia pastoris.BioMed research international · 2015Article
- Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production.Applied microbiology and biotechnology · 2014Review
- Extensive expansion of A1 family aspartic proteinases in fungi revealed by evolutionary analyses of 107 complete eukaryotic proteomes.Genome biology and evolution · 2014Article
- Improvement of catalytic efficiency and thermostability of recombinant Streptomyces griseus trypsin by introducing artificial peptide.World journal of microbiology & biotechnology · 2014Article
- Cloning and characterization of the glycoside hydrolases that remove xylosyl groups from 7-β-xylosyl-10-deacetyltaxol and its analogues.Molecular & cellular proteomics : MCP · 2013Article
- Disruption of YPS1 and PEP4 genes reduces proteolytic degradation of secreted HSA/PTH in Pichia pastoris GS115.Journal of industrial microbiology & biotechnology · 2013Article
- Rational design of a novel propeptide for improving active production of Streptomyces griseus trypsin in Pichia pastoris.Applied and environmental microbiology · 2013Article
- A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis.FEMS yeast research · 2011Article
- Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris.BMC microbiology · 2008Article
- Production of protein-based polymers in Pichia pastoris.Biotechnology advancesReview
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterologous proteins secreted by yeast and fungal expression hosts are occasionally degraded at basic amino acids. We cloned Pichia pastoris homologs of the Saccharomyces cerevisiae basic residue-specific endoproteases Kex2 and Yps1 to evaluate their involvement in the degradation of a secreted mammalian gelatin. Disruption of the P. pastoris KEX2 gene prevented proteolysis of the foreign protein at specific monoarginylic sites. The S. cerevisiae alpha-factor preproleader used to direct high-level gelatin secretion was correctly processed at its dibasic site in the absence of the prototypical proprotein convertase Kex2. Disruption of the YPS1 gene had no effect on gelatin degradation or processing of the alpha-factor propeptide. When both the KEX2 and YPS1 genes were disrupted, correct precursor maturation no longer occurred. The different substrate specificities of both proteases and their mutual redundancy for propeptide processing indicate that P. pastoris kex2 and yps1 single-gene disruptants can be used for the alpha-factor leader-directed secretion of heterologous proteins otherwise degraded at basic residues.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.