Enhancing co-translational folding of heterologous protein by deleting non-essential ribosomal proteins in Pichia pastoris View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Xihao Liao, Jing Zhao, Shuli Liang, Jingjie Jin, Cheng Li, Ruiming Xiao, Lu Li, Meijin Guo, Gong Zhang, Ying Lin

ABSTRACT

Background: Translational regulation played an important role in the correct folding of heterologous proteins to form bioactive conformations during biogenesis. Translational pausing coordinates protein translation and co-translational folding. Decelerating translation elongation speed has been shown to improve the soluble protein yield when expressing heterologous proteins in industrial expression hosts. However, rational redesign of translational pausing via synonymous mutations may not be feasible in many cases. Our goal was to develop a general and convenient strategy to improve heterologous protein synthesis in Pichia pastoris without mutating the expressed genes. Results: Here, a large-scale deletion library of ribosomal protein (RP) genes was constructed for heterologous protein expression in Pichia pastoris, and 59% (16/27) RP deletants have significantly increased heterologous protein yield. This is due to the delay of 60S subunit assembly by deleting non-essential ribosomal protein genes or 60S subunit processing factors, thus globally decreased the translation elongation speed and improved the co-translational folding, without perturbing the relative transcription level and translation initiation. Conclusion: Global decrease in the translation elongation speed by RP deletion enhanced co-translational folding efficiency of nascent chains and decreased protein aggregates to improve heterologous protein yield. A potential expression platform for efficient pharmaceutical proteins and industrial enzymes production was provided without synonymous mutation. More... »

PAGES

38

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1186/s13068-019-1377-z

    DOI

    http://dx.doi.org/10.1186/s13068-019-1377-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1112292060

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30828383


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