Evidence map›Paper›PMID 32313034›Full record

ArticleNature communications2020

A fully orthogonal system for protein synthesis in bacterial cells.

Nikolay A Aleksashin, Teresa Szal, Anne E d'Aquino, Michael C Jewett, Nora Vázquez-Laslop, Alexander S Mankin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  12. Noise Reduction in Resource-Coupled Multi-Module Gene Circuits through Antithetic Feedback Control.Proceedings of the ... IEEE Conference on Decision & Control. IEEE Conference on Decision & Control · 2024
    Article
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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 2 institutions in 1 country.

Nikolay A AleksashinCenter for Biomolecular Sciences, University of Illinois at Chicago, Chicago, IL, 60607, USA.ORCID http://orcid.org/0000-0002-3403-7587
Teresa SzalCenter for Biomolecular Sciences, University of Illinois at Chicago, Chicago, IL, 60607, USA.
Anne E d'AquinoInterdisciplinary Biological Science Program, Northwestern University, 2145 Sheridan Rd, Evanston, IL, 60208, USA.
Michael C JewettDepartment of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Rd, Evanston, IL, 60208, USA.ORCID http://orcid.org/0000-0003-2948-6211
Nora Vázquez-LaslopCenter for Biomolecular Sciences, University of Illinois at Chicago, Chicago, IL, 60607, USA.ORCID http://orcid.org/0000-0003-2256-693X
Alexander S MankinCenter for Biomolecular Sciences, University of Illinois at Chicago, Chicago, IL, 60607, USA. shura@uic.edu.ORCID http://orcid.org/0000-0002-3301-827X
University of Illinois Chicago · USNorthwestern University · US

Funding

Unraveling context specificity of translation by elucidating the mechanism of action of auxiliary translation factorsR35GM127134 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ALEXANDER S MANKIN · 2018 to 2026
$3.2M
NIGMS NIH HHS R35 GM127134
6 · The paper itself

Abstract

Ribosome engineering is a powerful approach for expanding the catalytic potential of the protein synthesis apparatus. Due to the potential detriment the properties of the engineered ribosome may have on the cell, the designer ribosome needs to be functionally isolated from the translation machinery synthesizing cellular proteins. One solution to this problem was offered by Ribo-T, an engineered ribosome with tethered subunits which, while producing a desired protein, could be excluded from general translation. Here, we provide a conceptually different design of a cell with two orthogonal protein synthesis systems, where Ribo-T produces the proteome, while the dissociable ribosome is committed to the translation of a specific mRNA. The utility of this system is illustrated by generating a comprehensive collection of mutants with alterations at every rRNA nucleotide of the peptidyl transferase center and isolating gain-of-function variants that enable the ribosome to overcome the translation termination blockage imposed by an arrest peptide.

Indexed as

AllelesBacteriaCell-Free SystemCrystallography, X-RayModels, MolecularModels, TheoreticalMolecular ConformationMutationPeptidesPeptidyl TransferasesPlasmidsProtein BiosynthesisProtein EngineeringProteomeRibosomesRNA, MessengerPeptidesPeptidyl TransferasesProteomeRNA, MessengerRNA, RibosomalRNA, Ribosomal, 23S

Identifiers

PMID32313034
PMCPMC7170887
OpenAlexW3016820202

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.