ArticleeLife2014
mRNA-programmed translation pauses in the targeting of E. coli membrane proteins.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 91 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed.Nature structural & molecular biology · 2026Article
- Suboptimal codon pairs trigger ribosome collisions and cellular quality control responses in tRNA modification mutants.Nucleic acids research · 2025Article
- Codon usage bias in yeasts and its correlation with gene expression, growth temperature, and protein structure.Frontiers in microbiology · 2024Article
- Article
- Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The landscape of translational stall sites in bacteria revealed by monosome and disome profiling.RNA (New York, N.Y.) · 2022Article
- Deep conservation of ribosome stall sites across RNA processing genes.NAR genomics and bioinformatics · 2021Article
- The effects of codon bias and optimality on mRNA and protein regulation.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- Compensating Complete Loss of Signal Recognition Particle During Co-translational Protein Targeting by the Translation Speed and Accuracy.Frontiers in microbiology · 2021Article
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Ribosomal stalk proteins RPLP1 and RPLP2 promote biogenesis of flaviviral and cellular multi-pass transmembrane proteins.Nucleic acids research · 2020Article
- Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020Review
- A pair of non-optimal codons are necessary for the correct biosynthesis of theRoyal Society open science · 2019Article
- Article
- Optimization of carbon and energy utilization through differential translational efficiency.Nature communications · 2018Article
- Within-Gene Shine-Dalgarno Sequences Are Not Selected for Function.Molecular biology and evolution · 2018Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Development of a generic β-lactamase screening system for improved signal peptides for periplasmic targeting of recombinant proteins in Escherichia coli.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all living organisms, ribosomes translating membrane proteins are targeted to membrane translocons early in translation, by the ubiquitous signal recognition particle (SRP) system. In eukaryotes, the SRP Alu domain arrests translation elongation of membrane proteins until targeting is complete. Curiously, however, the Alu domain is lacking in most eubacteria. In this study, by analyzing genome-wide data on translation rates, we identified a potential compensatory mechanism in E. coli that serves to slow down the translation during membrane protein targeting. The underlying mechanism is likely programmed into the coding sequence, where Shine-Dalgarno-like elements trigger elongation pauses at strategic positions during the early stages of translation. We provide experimental evidence that slow translation during targeting and improves membrane protein production fidelity, as it correlates with better folding of overexpressed membrane proteins. Thus, slow elongation is important for membrane protein targeting in E. coli, which utilizes mechanisms different from the eukaryotic one to control the translation speed.
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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.