Evidence map›Paper›PMID 28158713›Full record

ArticleNucleic acids research2017

Precise quantification of translation inhibition by mRNA structures that overlap with the ribosomal footprint in N-terminal coding sequences.

Amin Espah Borujeni, Daniel Cetnar, Iman Farasat, Ashlee Smith, Natasha Lundgren, Howard M Salis

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

84 citing papers in PubMed, 165 citations in OpenAlex.

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  16. High-Throughput Tiling of Essential mRNAs Increases Potency of Antisense Antibiotics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Amin Espah BorujeniDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Daniel CetnarDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Iman FarasatDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Ashlee SmithDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Natasha LundgrenDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Howard M SalisDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A mRNA's translation rate is controlled by several sequence determinants, including the presence of RNA structures within the N-terminal regions of its coding sequences. However, the physical rules that govern when such mRNA structures will inhibit translation remain unclear. Here, we introduced systematically designed RNA hairpins into the N-terminal coding region of a reporter protein with steadily increasing distances from the start codon, followed by characterization of their mRNA and expression levels in Escherichia coli. We found that the mRNAs' translation rates were repressed, by up to 530-fold, when mRNA structures overlapped with the ribosome's footprint. In contrast, when the mRNA structure was located outside the ribosome's footprint, translation was repressed by <2-fold. By combining our measurements with biophysical modeling, we determined that the ribosomal footprint extends 13 nucleotides into the N-terminal coding region and, when a mRNA structure overlaps or partially overlaps with the ribosomal footprint, the free energy to unfold only the overlapping structure controlled the extent of translation repression. Overall, our results provide precise quantification of the rules governing translation initiation at N-terminal coding regions, improving the predictive design of post-transcriptional regulatory elements that regulate translation rate.

Indexed as

Protein BiosynthesisBase SequenceBiophysical PhenomenaGene ExpressionNucleic Acid ConformationOpen Reading FramesPeptide Chain Initiation, TranslationalRibosomesRNA, MessengerThermodynamicsRNA, Messenger

Identifiers

PMID28158713
PMCPMC5435973
OpenAlexW2952214797

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.