Evidence map›Paper›PMID 18215412›Full record

ArticleBioorganic chemistry2008

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi.

Jason M Crawford, Anna L Vagstad, Kenneth C Ehrlich, Craig A Townsend

Abstract read
In one paragraph

Article in Bioorganic chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.3field-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

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Biosynthesis of Cytosporones in Leotiomycetous Filamentous Fungi.Journal of the American Chemical Society · 2024
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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

4 authors at 2 institutions in 1 country.

Jason M CrawfordDepartment of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Anna L Vagstad
Kenneth C Ehrlich
Craig A Townsend
Johns Hopkins University · USSouthern Regional Research Center · US

Funding

Iterative Polyketide Synthase Function, Structure and PathwaysR01ES001670 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI TOWNSEND, CRAIG ARTHUR · 1985 to 2023
$9.2M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
NIEHS NIH HHS ES 001670NIEHS NIH HHS R01 ES001670NIGMS NIH HHS T32 GM080189
6 · The paper itself

Abstract

Search of the protein database with the aflatoxin pathway polyketide synthase (PKS) revealed putative PKSs in the pathogenic fungi Coccidioides immitis and Coccidioides posadasii that could require partnerships with a pair of fatty acid synthase (FAS) subunits for the biosynthesis of fatty acid-polyketide hybrid metabolites. A starter unit:acyl-carrier protein transacylase (SAT) domain was discovered in the nonreducing PKS. This domain is thought to accept the fatty acid product from the FAS to initiate polyketide synthesis. We expressed the C. immitis SAT domain in Escherichia coli and showed that this domain, unlike that from the aflatoxin pathway PKS, transferred octanoyl-CoA four times faster than hexanoyl-CoA. The SAT domain also formed a covalent octanoyl intermediate and transferred this group to a free-standing ACP domain. Our results suggest that C. immitis/posadasii, both human fungal pathogens, contain a FAS/PKS cluster with functional similarity to the aflatoxin cluster found in Aspergillus species. Dissection of the PKS and determination of in vitro SAT domain specificity provides a tool to uncover the growing number of similar sequenced pathways in fungi, and to guide elucidation of the fatty acid-polyketide hybrid metabolites that they produce.

Indexed as

Genome, FungalAcyl Coenzyme AAcyltransferasesAflatoxinsBinding SitesCoccidioidesDatabases, ProteinEscherichia coliFatty AcidsFatty Acid SynthasesPolyketide SynthasesProtein Structure, TertiarySignal TransductionSubstrate SpecificityAcyl Coenzyme AAcyltransferasesAflatoxinsFatty AcidsFatty Acid Synthasesoctanoyl-coenzyme APolyketide Synthases

Identifiers

PMID18215412
PMCPMC3200548
OpenAlexW2076230762

What OpenQuestion holds

Textmetadata
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.