Evidence map›Paper›PMID 30183279›Full record

ArticleJournal of the American Chemical Society2018

Rapid Screening of Lanthipeptide Analogs via In-Colony Removal of Leader Peptides in Escherichia coli.

Tong Si, Qiqi Tian, Yuhao Min, Linzixuan Zhang, Jonathan V Sweedler, Wilfred A van der Donk, Huimin Zhao

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Tong SiCarl R. Woese Institute for Genomic Biology , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0003-2985-9014
Qiqi TianDepartment of Biochemistry , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.
Yuhao MinDepartment of Chemistry , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.
Linzixuan ZhangDepartment of Chemistry , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.
Jonathan V SweedlerCarl R. Woese Institute for Genomic Biology , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0003-3107-9922
Wilfred A van der DonkCarl R. Woese Institute for Genomic Biology , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0002-5467-7071
Huimin ZhaoCarl R. Woese Institute for Genomic Biology , University of Illinois at Urbana-Champaign , Urbana , Illinois 61801 , United States.ORCID 0000-0002-9069-6739
University of Illinois Urbana-Champaign · USHoward Hughes Medical Institute · US

Funding

Structural Elucidation and Biosynthesis P01GM077596 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI METCALF, WILLIAM W · 2007 to 2016
$15.3M
Posttranslational Modifications in Natural Product BiosynthesisR01GM058822 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 1999 to 2015
$3.8M
Posttranslational Modifications during Natural Product BiosynthesisR37GM058822 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2016 to 2025
$2.9M
NIGMS NIH HHS P01 GM077596NIGMS NIH HHS R01 GM058822NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

Most native producers of ribosomally synthesized and post-translationally modified peptides (RiPPs) utilize N-terminal leader peptides to avoid potential cytotoxicity of mature products to the hosts. Unfortunately, the native machinery of leader peptide removal is often difficult to reconstitute in heterologous hosts. Here we devised a general method to produce bioactive lanthipeptides, a major class of RiPP molecules, in Escherichia coli colonies using synthetic biology principles, where leader peptide removal is programmed temporally by protease compartmentalization and inducible cell autolysis. We demonstrated the method for producing two lantibiotics, haloduracin and lacticin 481, and performed analog screening for haloduracin. This method enables facile, high throughput discovery, characterization, and engineering of RiPPs.

Indexed as

BacteriocinsEscherichia coliGene Transfer TechniquesLactococcus lactisPlasmidsProtein EngineeringProtein Processing, Post-TranslationalProtein Sorting SignalsBacteriocinshaloduracin, Bacillus haloduranslacticin 481Protein Sorting Signals

Identifiers

PMID30183279
PMCPMC6476326
OpenAlexW2890919892

What OpenQuestion holds

Textmetadata
LicenceTDM
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.