Evidence map›Paper›PMID 28240912›Full record

ArticleJournal of the American Chemical Society2017

Domain-Targeted Metabolomics Delineates the Heterocycle Assembly Steps of Colibactin Biosynthesis.

Eric P Trautman, Alan R Healy, Emilee E Shine, Seth B Herzon, Jason M Crawford

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

26 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Current understandings of colibactin regulation.Microbiology (Reading, England) · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. Organic letters · 2021
    Article
  7. Review
  8. Review
  9. Structure and bioactivity of colibactin.Bioorganic & medicinal chemistry letters · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. GenotoxicComparative medicine · 2019
    Article
  18. Refining and expanding nonribosomal peptide synthetase function and mechanism.Journal of industrial microbiology & biotechnology · 2019
    Review
  19. Article
  20. Review
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

5 authors at 1 institution in 1 country.

Eric P TrautmanDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.ORCID 0000-0002-0974-2356
Alan R HealyDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.
Emilee E ShineChemical Biology Institute, Yale University , West Haven, Connecticut 06516, United States.
Seth B HerzonDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.ORCID 0000-0001-5940-9853
Jason M CrawfordDepartment of Chemistry, Yale University , New Haven, Connecticut 06520, United States.ORCID 0000-0002-7583-1242
Yale University · US

Funding

Cryptic gut bacterial metabolites that regulate colorectal cancer formationDP2CA186575 · NCI · YALE UNIVERSITY · PI CRAWFORD, JASON MICHAEL · 2013 to 2013
$2.5M
Synthesis and Study of Complex Antiproliferative and Antimalarial Natural ProductsR01GM110506 · NIGMS · YALE UNIVERSITY · PI HERZON, SETH B. · 2015 to 2018
$1.2M
NCI NIH HHS DP2 CA186575NIGMS NIH HHS R01 GM110506
6 · The paper itself

Abstract

Modular polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) comprise giant multidomain enzymes responsible for the "assembly line" biosynthesis of many genetically encoded small molecules. Site-directed mutagenesis, protein biochemical, and structural studies have focused on elucidating the catalytic mechanisms of individual multidomain proteins and protein domains within these megasynthases. However, probing their functions at the cellular level typically has invoked the complete deletion (or overexpression) of multidomain-encoding genes or combinations of genes and comparing those mutants with a control pathway. Here we describe a "domain-targeted" metabolomic strategy that combines genome editing with pathway analysis to probe the functions of individual PKS and NRPS catalytic domains at the cellular metabolic level. We apply the approach to the bacterial colibactin pathway, a genotoxic NRPS-PKS hybrid pathway found in certain Escherichia coli. The pathway produces precolibactins, which are converted to colibactins by a dedicated peptidase, ClbP. Domain-targeted metabolomics enabled the characterization of "multidomain signatures", or functional readouts of NRPS-PKS domain contributions to the pathway-dependent metabolome. These multidomain signatures provided experimental support for individual domain contributions to colibactin biosynthesis and delineated the assembly line timing events of colibactin heterocycle formation. The analysis also led to the structural characterization of two reactive precolibactin metabolites. We demonstrate the fate of these reactive intermediates in the presence and absence of ClbP, which dictates the formation of distinct product groups resulting from alternative cyclization cascades. In the presence of the peptidase, the reactive intermediates are converted to a known genotoxic scaffold, providing metabolic support of our mechanistic model for colibactin-induced genotoxicity. Domain-targeted metabolomics could be more widely used to characterize NRPS-PKS pathways with unprecedented genetic and metabolic precision.

Indexed as

MetabolomicsEscherichia coliHeterocyclic CompoundsMolecular ConformationPeptidesPeptide SynthasesPolyketidesPolyketide SynthasescolibactinHeterocyclic Compoundsnon-ribosomal peptide synthasePeptidesPeptide SynthasesPolyketidesPolyketide Synthases

Identifiers

PMID28240912
PMCPMC5831107
OpenAlexW2594735183

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.