ArticleNucleic acids research2012
Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- Construction of primary chassis cells with efficient protein expression in Thermus thermophilus.Microbial cell factories · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Thermostable in vitro transcription-translation compatible with microfluidic droplets.Microbial cell factories · 2024Article
- Solid-Phase Cell-Free Protein Synthesis and Its Applications in Biotechnology.Advances in biochemical engineering/biotechnology · 2023Article
- Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022Article
- Biotechnology Applications of Cell-Free Expression Systems.Life (Basel, Switzerland) · 2021Review
- Differential Contribution of Protein Factors and 70S Ribosome to Elongation.International journal of molecular sciences · 2021Article
- Kinetic Analysis Suggests Evolution of Ribosome Specificity in Modern Elongation Factor-Tus from "Generalist" Ancestors.Molecular biology and evolution · 2021Article
- In Vitro Reconstitution of Yeast Translation System Capable of Synthesizing Long Polypeptide and Recapitulating Programmed Ribosome Stalling.Methods and protocols · 2021Article
- Ancestral Sequence Reconstruction: From Chemical Paleogenetics to Maximum Likelihood Algorithms and Beyond.Journal of molecular evolution · 2021Article
- Occurrence of randomly recombined functional 16S rRNA genes in Thermus thermophilus suggests genetic interoperability and promiscuity of bacterial 16S rRNAs.Scientific reports · 2019Article
- Flexizyme-Enabled Benchtop Biosynthesis of Thiopeptides.Journal of the American Chemical Society · 2019Article
- Regulatory Factors for tRNA Modifications in Extreme- Thermophilic BacteriumFrontiers in genetics · 2019Review
- Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.Structure (London, England : 1993) · 2018Article
- In vitro transcription-translation using bacterial genome as a template to reconstitute intracellular profile.Nucleic acids research · 2017Article
- Functional Constraints on Replacing an Essential Gene with Its Ancient and Modern Homologs.mBio · 2017Article
- Experimental Evolution of Escherichia coli Harboring an Ancient Translation Protein.Journal of molecular evolution · 2017Article
- Are in vivo selections on the path to extinction?Microbial biotechnology · 2017Article
- Article
- Engineering bacterial transcription regulation to create a synthetic in vitro two-hybrid system for protein interaction assays.Journal of the American Chemical Society · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Thermus thermophilus is a thermophilic model organism distantly related to the mesophilic model organism E. coli. We reconstituted protein translation of Thermus thermophilus in vitro from purified ribosomes, transfer ribonucleic acids (tRNAs) and 33 recombinant proteins. This reconstituted system was fully functional, capable of translating natural messenger RNA (mRNA) into active full-length proteins at temperatures up to 65°C and with yields up to 60 μg/ml. Surprisingly, the synthesis of active proteins also occurred at 37°C, a temperature well below the minimal growth temperature for T. thermophilus. A polyamine was required, with tetraamine being most effective, for translation at both high and low temperatures. Using such a defined in vitro system, we demonstrated a minimal set of components that are sufficient for synthesizing active proteins at high temperatures, the functional compatibility of key translation components between T. thermophilus and E. coli, and the functional conservation of a number of resurrected ancient elongation factors. This work sets the stage for future experiments that apply abundant structural information to biochemical characterization of protein translation and folding in T. thermophilus. Because it contains significantly reduced nucleases and proteases, this reconstituted thermostable cell-free protein synthesis system may enable in vitro engineering of proteins with improved thermostability.
Indexed as
Identifiers
What 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.