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An improved secretion signal enhances the secretion of model proteins from Pichia pastoris.

Juan J Barrero | Jason C Casler | Francisco Valero | Pau Ferrer | Benjamin S Glick
Microbial cell factories | 2018

Proteins can be secreted from a host organism with the aid of N-terminal secretion signals. The budding yeast Pichia pastoris (Komagataella sp.) is widely employed to secrete proteins of academic and industrial interest. For this yeast, the most commonly used secretion signal is the N-terminal portion of pre-pro-α-factor from Saccharomyces cerevisiae. However, this secretion signal promotes posttranslational translocation into the endoplasmic reticulum (ER), so proteins that can fold in the cytosol may be inefficiently translocated and thus poorly secreted. In addition, if a protein self-associates, the α-factor pro region can potentially cause aggregation, thereby hampering export from the ER. This study addresses both limitations of the pre-pro-α-factor secretion signal.

Pubmed ID: 30314480

Research resources used in this publication

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Associated grants

  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM104010

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