ArticlePeerJ2015
Tunable translational control using site-specific unnatural amino acid incorporation in Escherichia coli.
Article in PeerJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed.
- Optimization Strategy of Expression Vectors and Regulatory Elements for Enhanced Protein Production inInternational journal of molecular sciences · 2025Review
- Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology.Chemical reviews · 2024Review
- A novel vaccine strategy using quick and easy conversion of bacterial pathogens to unnatural amino acid-auxotrophic suicide derivatives.Microbiology spectrum · 2024Article
- An Unnatural Amino Acid-Regulated Growth Controller Based on Informational Disturbance.Life (Basel, Switzerland) · 2021Article
- Titrating bacterial growth and chemical biosynthesis for efficient N-acetylglucosamine and N-acetylneuraminic acid bioproduction.Nature communications · 2020Article
- Extremely Low Leakage Expression Systems Using Dual Transcriptional-Translational Control for Toxic Protein Production.International journal of molecular sciences · 2020Review
- Translational Control using an Expanded Genetic Code.International journal of molecular sciences · 2019Review
- An engineered bacterium auxotrophic for an unnatural amino acid: a novel biological containment system.PeerJ · 2015Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation of target gene transcripts in Escherichia coli harboring UAG amber stop codons can be switched on by the amber-codon-specific incorporation of an exogenously supplied unnatural amino acid, 3-iodo-L-tyrosine. Here, we report that this translational switch can control the translational efficiency at any intermediate magnitude by adjustment of the 3-iodo-L-tyrosine concentration in the medium, as a tunable translational controller. The translational efficiency of a target gene reached maximum levels with 10(-5) M 3-iodo-L-tyrosine, and intermediate levels were observed with suboptimal concentrations (approximately spanning a 2-log10 concentration range, 10(-7)-10(-5) M). Such intermediate-level expression was also confirmed in individual bacteria.
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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.