ArticlePLoS genetics2012
Broad-specificity mRNA-rRNA complementarity in efficient protein translation.
Article in PLoS genetics, 2012. 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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Who cites it
8 citing papers in PubMed.
- Expression of distinct maternal and somatic 5.8S, 18S, and 28S rRNA types during zebrafish development.RNA (New York, N.Y.) · 2017Article
- The 5΄ UTR of the type I toxin ZorO can both inhibit and enhance translation.Nucleic acids research · 2017Article
- Application of sorting and next generation sequencing to study 5΄-UTR influence on translation efficiency in Escherichia coli.Nucleic acids research · 2017Article
- The coding and noncoding architecture of the Caulobacter crescentus genome.PLoS genetics · 2014Article
- An RNA-seq method for defining endoribonuclease cleavage specificity identifies dual rRNA substrates for toxin MazF-mt3.Nature communications · 2014Article
- Evidence for context-dependent complementarity of non-Shine-Dalgarno ribosome binding sites to Escherichia coli rRNA.ACS chemical biology · 2013Article
- Sounds of silence: synonymous nucleotides as a key to biological regulation and complexity.Nucleic acids research · 2013Review
- Article
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Authors and funding
4 authors.
Funding
Abstract
Studies of synthetic, well-defined biomolecular systems can elucidate inherent capabilities that may be difficult to uncover in a native biological context. Here, we used a minimal, reconstituted translation system from Escherichia coli to identify efficient ribosome binding sites (RBSs) in an unbiased, high-throughput manner. We applied ribosome display, a powerful in vitro selection method, to enrich only those mRNA sequences which could direct rapid protein translation. In addition to canonical Shine-Dalgarno (SD) motifs, we unexpectedly recovered highly efficient cytosine-rich (C-rich) sequences that exhibit unmistakable complementarity to the 16S rRNA of the small subunit of the ribosome, indicating that broad-specificity base-pairing may be an inherent, general mechanism for efficient translation. Furthermore, given the conservation of ribosomal structure and function across species, the broader relevance of C-rich RBS sequences identified through our in vitro evolution approach is supported by multiple, diverse examples in nature, including C-rich RBSs in several bacteriophage and plants, a poly-C consensus before the start codon in a lower eukaryote, and Kozak-like sequences in vertebrates.
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Registered trials
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