ArticleScientific reports2022
Expanding luciferase reporter systems for cell-free protein expression.
Article in Scientific reports, 2022. 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, 13 citations in OpenAlex.
- Protocellular energy transduction, information and fitness.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Simultaneous in vitro expression of minimal 21 transfer RNAs by tRNA array method.Nature communications · 2025Article
- Chloroplast Cell-Free Systems from Different Plant Species as a Rapid Prototyping Platform.ACS synthetic biology · 2024Article
- Improvement in Tol2 transposon for efficient large-cargo capacity transgene applications in cultured cells and zebrafish (Zoological research · 2024Article
- HPLC for at-line reaction monitoring and purification improves yield and purity of tRNA.Frontiers in molecular biosciences · 2024Article
- Cell-free transcription-translation system: a dual read-out assay to characterize riboswitch function.Nucleic acids research · 2023Article
- Rapid and Finely-Tuned Expression for Deployable Sensing Applications.Advances in biochemical engineering/biotechnology · 2023Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Luciferases are often used as a sensitive, versatile reporter in cell-free transcription-translation (TXTL) systems, for research and practical applications such as engineering genetic parts, validating genetic circuits, and biosensor outputs. Currently, only two luciferases (Firefly and Renilla) are commonly used without substrate cross-talk. Here we demonstrate the expansion of the cell-free luciferase reporter system, with two orthogonal luciferase reporters: N. nambi luciferase (Luz) and LuxAB. These luciferases do not have cross-reactivity with the Firefly and Renilla substrates. We also demonstrate a substrate regeneration pathway for one of the new luciferases, enabling long-term time courses of protein expression monitoring in the cell-free system. Furthermore, we reduced the number of genes required in TXTL expression, by engineering a cell extract containing part of the luciferase enzymes. Our findings lead to an expanded platform with multiple orthogonal luminescence translation readouts for in vitro protein expression.
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