Evidence map›Paper›PMID 30821147›Full record

ArticleBiochemistry2019

Identification of the Functional Roles of Six Key Proteins in the Biosynthesis of Enterobacteriaceae Colanic Acid.

Phillip M Scott, Katelyn M Erickson, Jerry M Troutman

Abstract read
In one paragraph

Article in Biochemistry, 2019. 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
3.3field-weighted citation impact, top 8% 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, 44 citations in OpenAlex.

  1. Article
  2. WrtF fromProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. An exopolysaccharide pathway from a freshwaterJournal of bacteriology · 2024
    Article
  7. Article
  8. Diagnostics (Basel, Switzerland) · 2024
    Article
  9. Article
  10. A novel exopolysaccharide pathway from a freshwaterbioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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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

3 authors at 1 institution in 1 country.

Phillip M Scott
Katelyn M Erickson
University of North Carolina at Charlotte · US

Funding

In vitro and Cellular Tools for Complex Polysaccharide BiosynthesisR01GM123251 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI TROUTMAN, JERRY M · 2017 to 2023
$2.1M
Toolkit development for bacterial isoprenoid utilizing enzymesR15GM114773 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI TROUTMAN, JERRY M · 2015 to 2015
$350k
NIGMS NIH HHS R01 GM123251NIGMS NIH HHS R15 GM114773
6 · The paper itself

Abstract

When subjected to harsh conditions such as low pH, pathogenic Escherichia coli can secrete colanic acid to establish a protective barrier between the organism and the acidic environment. The colanic acid consists of a six-sugar repeating unit polymer comprised of glucose, fucose, galactose, and glucuronic acid. The region of the E. coli genome that encodes colanic acid biosynthesis has been reported, and the first enzyme in the biosynthesis pathway has been biochemically characterized. However, the specific roles of the remaining genes required for colanic acid biosynthesis have not been identified. Here we report the in vitro reconstitution of the next six steps in the assembly of the colanic acid repeating unit. To do this, we have cloned and overexpressed each gene within the colanic acid biosynthesis operon. We then tested the activity of the protein product of these genes using high-performance liquid chromatography analysis and a fluorescent analogue of the isoprenoid anchor bactoprenyl diphospho-glucose as a starting substrate. To ensure that retention time changes were associated with varying sugar additions or modifications, we developed a liquid chromatography-mass spectrometry method for analysis of the products produced by each enzyme. We have identified the function of all but one encoded glycosyltransferase and have identified the function of two acetyltransferases. This work demonstrates the centrality of acetylation in the biosynthesis of colanic acid and provides insight into the activity of key proteins involved in the production of an important and highly conserved bacterial glycopolymer.

Indexed as

Biosynthetic PathwaysAcetylationBacterial ProteinsCloning, MolecularEnterobacteriaceaeEscherichia coliGenes, BacterialGlycosyltransferasesPolysaccharidesBacterial Proteinscolanic acidGlycosyltransferasesPolysaccharides

Identifiers

PMID30821147
PMCPMC6445743
OpenAlexW2920590876

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.