ArticleNature chemical biology2018
Synthetic microbial consortia enable rapid assembly of pure translation machinery.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed.
- Multiple Adenylate-Forming Enzymes Contribute to Biosynthesis of the DPO Quorum-Sensing Autoinducer.ACS chemical biology · 2026Article
- Improving cellulosic ethanol production by an engineered yeast consortium displaying a pentafunctional mini-cellulosome.FEMS yeast research · 2025Article
- ATP Regeneration from Pyruvate in the PURE System.ACS synthetic biology · 2025Article
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- A systematic discussion and comparison of the construction methods of synthetic microbial community.Synthetic and systems biotechnology · 2024Review
- Engineering living materials by synthetic biology.Biophysics reviews · 2023Review
- On-demand biomanufacturing through synthetic biology approach.Materials today. Bio · 2023Article
- Cell-Free Display Techniques for Protein Evolution.Advances in biochemical engineering/biotechnology · 2023Article
- Dynamic cybergenetic control of bacterial co-culture composition via optogenetic feedback.Nature communications · 2022Article
- Engineering consortia by polymeric microbial swarmbots.Nature communications · 2022Article
- In vitro reconstitution of the Escherichia coli 70S ribosome with a full set of recombinant ribosomal proteins.Journal of biochemistry · 2022Article
- High-Throughput Experimentation Using Cell-Free Protein Synthesis Systems.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cell-Free PURE System: Evolution and Achievements.Biodesign research · 2022Review
- Biochemistry of Aminoacyl tRNA Synthetase and tRNAs and Their Engineering for Cell-Free and Synthetic Cell Applications.Frontiers in bioengineering and biotechnology · 2022Review
- Engineered microbial consortia: strategies and applications.Microbial cell factories · 2021Review
- Decentralizing Cell-Free RNA Sensing With the Use of Low-Cost Cell Extracts.Frontiers in bioengineering and biotechnology · 2021Article
- Cell-free biology using remote-controlled digital microfluidics for individual droplet control.RSC advances · 2020Article
- Holistic engineering of cell-free systems through proteome-reprogramming synthetic circuits.Nature communications · 2020Article
- Article
- Strategies for in vitro engineering of the translation machinery.Nucleic acids research · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of recombinant multiprotein systems requires multiple culturing and purification steps that scale linearly with the number of constituent proteins. This problem is particularly pronounced in the preparation of the 34 proteins involved in transcription and translation systems, which are fundamental biochemistry tools for reconstitution of cellular pathways ex vivo. Here, we engineer synthetic microbial consortia consisting of between 15 and 34 Escherichia coli strains to assemble the 34 proteins in a single culturing, lysis, and purification procedure. The expression of these proteins is controlled by synthetic genetic modules to produce the proteins at the correct ratios. We show that the pure multiprotein system is functional and reproducible, and has low protein contaminants. We also demonstrate its application in the screening of synthetic promoters and protease inhibitors. Our work establishes a novel strategy for producing pure translation machinery, which may be extended to the production of other multiprotein systems.
Indexed as
Identifiers
29131146What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.