Evidence map›Paper›PMID 16906151›Full record

ArticleNature chemical biology2006

Biosynthesis of Dictyostelium discoideum differentiation-inducing factor by a hybrid type I fatty acid-type III polyketide synthase.

Michael B Austin, Tamao Saito, Marianne E Bowman, Stephen Haydock, Atsushi Kato, Bradley S Moore, Robert R Kay, Joseph P Noel

Abstract read
In one paragraph

Article in Nature chemical biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
8.3field-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

49 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Global profiling of polyketide synthases in facultative multicellular eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. The Amoeba Dictyostelium discoideum as Novel Production Host for Complex Substances.Advances in biochemical engineering/biotechnology · 2025
    Review
  8. Isolation and Structure Determination of New Pyrones fromMolecules (Basel, Switzerland) · 2024
    Article
  9. Generating polyketide diversity inProceedings. Biological sciences · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Nostopeptolide plays a governing role during cellular differentiation of the symbiotic cyanobacterium Nostoc punctiforme.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 6 institutions in 3 countries.

Michael B AustinHoward Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies, La Jolla, California 92037, USA.
Tamao Saito
Marianne E Bowman
Stephen Haydock
Atsushi Kato
Bradley S Moore
Robert R Kay
Joseph P Noel
Hokkaido University · JPHoward Hughes Medical Institute · USMRC Laboratory of Molecular Biology · GBSalk Institute for Biological Studies · USScripps Institution of Oceanography · USUniversity of Cambridge · GB

Funding

Type III Polyketide Synthases: Structure and MechanismR01AI052443 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MOORE, BRADLEY S · 2002 to 2006
$1.7M
Howard Hughes Medical InstituteMedical Research Council MC_U105115237NIAID NIH HHS AI52443NIAID NIH HHS R01 AI052443
6 · The paper itself

Abstract

Differentiation-inducing factors (DIFs) are well known to modulate formation of distinct communal cell types from identical Dictyostelium discoideum amoebas, but DIF biosynthesis remains obscure. We report complimentary in vivo and in vitro experiments identifying one of two approximately 3,000-residue D. discoideum proteins, termed 'steely', as responsible for biosynthesis of the DIF acylphloroglucinol scaffold. Steely proteins possess six catalytic domains homologous to metazoan type I fatty acid synthases (FASs) but feature an iterative type III polyketide synthase (PKS) in place of the expected FAS C-terminal thioesterase used to off load fatty acid products. This new domain arrangement likely facilitates covalent transfer of steely N-terminal acyl products directly to the C-terminal type III PKS active sites, which catalyze both iterative polyketide extension and cyclization. The crystal structure of a steely C-terminal domain confirms conservation of the homodimeric type III PKS fold. These findings suggest new bioengineering strategies for expanding the scope of fatty acid and polyketide biosynthesis.

Indexed as

DictyosteliumAcyltransferasesAmino Acid SequenceAnimalsCatalytic DomainCloning, MolecularCrystallography, X-RayDimerizationFatty Acid SynthasesHexanonesHydrocarbons, ChlorinatedModels, MolecularMolecular Sequence DataMutationProtein ConformationProtozoan ProteinsAcyltransferasesDifferentiation-inducing factor-1, DictyosteliumFatty Acid Synthasesflavanone synthetaseHexanonesHydrocarbons, ChlorinatedProtozoan Proteins

Identifiers

PMID16906151
PMCPMC2864586
OpenAlexW1971770037

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.