ArticleBiotechnology for biofuels2019
Enhancing co-translational folding of heterologous protein by deleting non-essential ribosomal proteins in
Article in Biotechnology for biofuels, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Yarrowia lipolytica and Komagataella phaffii (Pichia pastoris) as Hosts for Heterologous Expression of Lipases.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Improvement of cannabichromenic acid synthase activity and construction of recombinant yeast strain.Archives of microbiology · 2026Article
- Characterizing heterologous protein burden in Komagataella phaffii.FEMS yeast research · 2025Article
- CRISPR-Cas9 knockout screen informs efficient reduction of the Komagataella phaffii secretome.Microbial cell factories · 2024Article
- CRISPR/Cas9-mediated point mutations improve α-amylase secretion in Saccharomyces cerevisiae.FEMS yeast research · 2022Article
- Comparative transcriptomic analysis-based identification of the regulation of foreign proteins with different stabilities expressed inFrontiers in microbiology · 2022Article
- A versatile toolbox for CRISPR-based genome engineering in Pichia pastoris.Applied microbiology and biotechnology · 2021Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTranslational 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
resultsHere, a large-scale deletion library of ribosomal protein (RP) genes was constructed for heterologous protein expression in
conclusionGlobal 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.
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