ArticleBMC biotechnology2014
Tobacco BY-2 cell-free lysate: an alternative and highly-productive plant-based in vitro translation system.
Article in BMC biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Eukaryotic cell-free protein synthesis: Chassis diversification, system engineering, and emerging applications.Synthetic and systems biotechnology · 2026Review
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- A Pichia pastoris Cell-Free Protein Synthesis Platform.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Online monitoring of the mitochondrial respiration activity and protein formation in the Almost Living Cell-free Expression (ALiCE) system.BMC biotechnology · 2025Article
- Proviral insights of glycolytic enolase inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- RH3 enhances antiviral defense by facilitating small RNA loading into Argonaute 2 at endoplasmic reticulum-chloroplast membrane contact sites.Nature communications · 2025Article
- BeyondChemical reviews · 2025Review
- Cell-Free Systems and Their Importance in the Study of Membrane Proteins.The Journal of membrane biology · 2025Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- OsAPSE modulates non-covalent interactions between arabinogalactan proteinFrontiers in plant science · 2025Article
- Review
- Review
- Promoting the production of challenging proteins via induced expression in CHO cells and modified cell-free lysates harboring T7 RNA polymerase and mutant eIF2α.Synthetic and systems biotechnology · 2024Article
- Green Biologics: Harnessing the Power of Plants to Produce Pharmaceuticals.International journal of molecular sciences · 2023Review
- Cell-Free Display Techniques for Protein Evolution.Advances in biochemical engineering/biotechnology · 2023Article
- Cell-Free Synthesis and Electrophysiological Analysis of Multipass Voltage-Gated Ion Channels Tethered in Microsomal Membranes.Advances in biochemical engineering/biotechnology · 2023Article
- Rapid screening and scaled manufacture of immunogenic virus-like particles in a tobacco BY-2 cell-free protein synthesis system.Frontiers in immunology · 2023Article
- Three Parts of the Plant Genome: On the Way to Success in the Production of Recombinant Proteins.Plants (Basel, Switzerland) · 2022Review
- Multiple Gene Expression in Cell-Free Protein Synthesis Systems for Reconstructing Bacteriophages and Metabolic Pathways.Microorganisms · 2022Review
- Optimising expression and extraction of recombinant proteins in plants.Frontiers in plant science · 2022Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundCell-free protein synthesis is a rapid and efficient method for the production of recombinant proteins. Usage of prokaryotic cell-free extracts often leads to non-functional proteins. Eukaryotic counterparts such as wheat germ extract (WGE) and rabbit reticulocyte lysate (RLL) may improve solubility and promote the correct folding of eukaryotic multi-domain proteins that are difficult to express in bacteria. However, the preparation of WGEs is complex and time-consuming, whereas RLLs suffer from low yields. Here we report the development of a novel cell-free system based on tobacco Bright Yellow 2 (BY-2) cells harvested in the exponential growth phase.
resultsThe highly-productive BY-2 lysate (BYL) can be prepared quickly within 4-5 h, compared to 4-5 d for WGE. The efficiency of the BYL was tested using three model proteins: enhanced yellow fluorescent protein (eYFP) and two versions of luciferase. The added mRNA was optimized by testing different 5' and 3' untranslated regions (UTRs). The protein yield in batch and dialysis reactions using BYL was much higher than that of a commercial Promega WGE preparation, achieving a maximum yield of 80 μg/mL of eYFP and 100 μg/mL of luciferase, compared to only 45 μg/mL of eYFP and 35 μg/mL of luciferase in WGEs. In dialysis reactions, the BYL yielded about 400 μg/mL eYFP, representing up to 50% more of the target protein than the Promega WGE, and equivalent to the amount using 5Prime WGE system.
conclusionsDue to the high yield and the short preparation time the BYL represents a remarkable improvement over current eukaryotic cell-free systems.
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