ArticleMicrobial cell factories2019
Fhl1p protein, a positive transcription factor in Pichia pastoris, enhances the expression of recombinant proteins.
Article in Microbial cell factories, 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.
- Overexpression of msnA reprograms metabolism to enhance recombinant protein secretion across Aspergillus species.Microbial cell factories · 2026Article
- Establishment and application of an RNAi system inFrontiers in bioengineering and biotechnology · 2025Article
- Combined strategies for improving the heterologous expression of a novel xylanase fromSynthetic and systems biotechnology · 2024Article
- IRES-mediated Pichia pastoris cell-free protein synthesis.Bioresources and bioprocessing · 2023Article
- Advances in Cell Engineering of theMetabolites · 2022Review
- Burden Imposed by Heterologous Protein Production in Two Major Industrial Yeast Cell Factories: Identifying Sources and Mitigation Strategies.Frontiers in fungal biology · 2022Review
- Establishing a EukaryoticFrontiers in bioengineering and biotechnology · 2020Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe methylotrophic yeast Pichia pastoris is well-known for the production of a broad spectrum of functional types of heterologous proteins including enzymes, antigens, engineered antibody fragments, and next gen protein scaffolds and many transcription factors are utilized to address the burden caused by the high expression of heterologous proteins. In this article, a novel P. pastoris transcription factor currently annotated as Fhl1p, an activator of ribosome biosynthesis processing, was investigated for promoting the expression of the recombinant proteins.
resultsThe function of Fhl1p of P. pastoris for improving the expression of recombinant proteins was verified in strains expressing phytase, pectinase and mRFP, showing that the productivity was increased by 20-35%. RNA-Seq was used to study the Fhl1p regulation mechanism in detail, confirming Fhl1p involved in the regulation of rRNA processing genes, ribosomal small/large subunit biogenesis genes, Golgi vesicle transport genes, etc., which contributed to boosting the expression of foreign proteins. The overexpressed Fhl1p strain exhibited increases in the polysome and monosome levels, showing improved translation activities.
conclusionThis study illustrated that the transcription factor Fhl1p could effectively enhance recombinant protein expression in P. pastoris. Furthermore, we provided the evidence that overexpressed Fhl1p was related to more active translation state.
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