Literature DB >> 7764684

Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae.

A S Robinson1, V Hines, K D Wittrup.   

Abstract

Overexpression of protein disulfide isomerase (PDI) from a single chromosomally integrated copy in Saccharomyces cerevisiae results in ten-fold higher levels of secretion of human platelet derived growth factor B homodimer, and a four-fold increase in secretion of Schizosaccharomyces pombe acid phosphatase. This result provides evidence that inefficient protein folding limits the secretion of some heterologous proteins, and that manipulation of the endoplasmic reticulum lumenal environment can help overcome this limitation.

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Year:  1994        PMID: 7764684     DOI: 10.1038/nbt0494-381

Source DB:  PubMed          Journal:  Biotechnology (N Y)        ISSN: 0733-222X


  51 in total

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4.  Engineering the protein secretory pathway of Saccharomyces cerevisiae enables improved protein production.

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Authors:  M M Harmsen; M I Bruyne; H A Raué; J Maat
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Review 8.  Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells.

Authors:  Aleš Berlec; Borut Strukelj
Journal:  J Ind Microbiol Biotechnol       Date:  2013-02-06       Impact factor: 3.346

9.  The ire1 and ptc2 genes involved in the unfolded protein response pathway in the filamentous fungus Trichoderma reesei.

Authors:  M Valkonen; M Penttilä; M Saloheimo
Journal:  Mol Genet Genomics       Date:  2004-10-08       Impact factor: 3.291

10.  Improvement of foreign-protein production in Aspergillus niger var. awamori by constitutive induction of the unfolded-protein response.

Authors:  Mari Valkonen; Michael Ward; Huaming Wang; Merja Penttilä; Markku Saloheimo
Journal:  Appl Environ Microbiol       Date:  2003-12       Impact factor: 4.792

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