ArticleScientific reports2017
A Novel Method to Evaluate Ribosomal Performance in Cell-Free Protein Synthesis Systems.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A detailed molecular picture of protein folding during active translation.bioRxiv : the preprint server for biology · 2026Article
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026Article
- Hydrogen/deuterium exchange mass spectrometry analysis of ribosome-nascent chain complexes to study protein biogenesis at the peptide level.Nature protocols · 2026Article
- Autonomous biogenesis of all thirty proteins of the Escherichia coli translation machinery.Nature communications · 2025Article
- Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide.Nucleic acids research · 2025Article
- Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025Review
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Impact of Molecule Concentration, Diffusion Rates and Surface Passivation on Single-Molecule Fluorescence Studies in Solution.Biomolecules · 2022Article
- The ribosome modulates folding inside the ribosomal exit tunnel.Communications biology · 2021Article
- Distinct pre-initiation steps in human mitochondrial translation.Nature communications · 2020Article
- Bottom-Up Construction of Complex Biomolecular Systems With Cell-Free Synthetic Biology.Frontiers in bioengineering and biotechnology · 2020Review
- Review
- Brightness-gated two-color coincidence detection unravels two distinct mechanisms in bacterial protein translation initiation.Communications biology · 2019Article
- Cell-Free Protein Synthesis From Fast-GrowingFrontiers in microbiology · 2018Article
- Cell-free protein synthesis from non-growing, stressed Escherichia coli.Scientific reports · 2017Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cell-free protein synthesis (CFPS) systems were designed to produce proteins with a minimal set of purified components, thus offering the possibility to follow translation as well as protein folding. In order to characterize the performance of the ribosomes in such a system, it is crucial to separately quantify the two main components of productivity, namely the fraction of active ribosomes and the number of synthesizing cycles. Here, we provide a direct and highly reliable measure of ribosomal activity in any given CFPS system, introducing an enhanced-arrest peptide variant. We observe an almost complete stalling of ribosomes that produce GFPem (~95%), as determined by common centrifugation techniques and fluorescence correlation spectroscopy (FCS). Moreover, we thoroughly study the effect of different ribosomal modifications independently on activity and number of synthesizing cycles. Finally, employing two-colour coincidence detection and two-colour colocalisation microscopy, we demonstrate real-time access to key productivity parameters with minimal sample consumption on a single ribosome level.
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