Evidence map›Paper›PMID 17360612›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Fusicoccins are biosynthesized by an unusual chimera diterpene synthase in fungi.

Tomonobu Toyomasu, Mai Tsukahara, Akane Kaneko, Rie Niida, Wataru Mitsuhashi, Tohru Dairi, Nobuo Kato, Takeshi Sassa

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 10% 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

76 citing papers in PubMed, 1 synthesis or guideline pooled it, 212 citations in OpenAlex.

  1. BioprospectingFrontiers in fungal biology · 2021
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Harnessing Genomics ofPlants (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Article
  8. Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Engineering substrate channeling in a bifunctional terpene synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Engineering Substrate Channeling in Assembly-Line Terpene Biosynthesis.bioRxiv : the preprint server for biology · 2024
    Article
  17. Review
  18. Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Tomonobu ToyomasuDepartment of Bioresource Engineering, Yamagata University, Tsuruoka, Yamagata 997-8555, Japan. toyomasu@tds1.tr.yamagata-u.ac.jp
Mai Tsukahara
Akane Kaneko
Rie Niida
Wataru Mitsuhashi
Tohru Dairi
Nobuo Kato
Takeshi Sassa
Yamagata University · JPOsaka Research Institute of Industrial Science and Technology · JPToyama Prefectural University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusicoccins are a class of diterpene glucosides produced by the plant-pathogenic fungus Phomopsis amygdali. As modulators of 14-3-3 proteins, fusicoccins function as potent activators of plasma membrane H(+)-ATPase in plants and also exhibit unique biological activity in animal cells. Despite their well studied biological activities, no genes encoding fusicoccin biosynthetic enzymes have been identified. Cyclic diterpenes are commonly synthesized via cyclization of a C(20) precursor, geranylgeranyl diphosphate (GGDP), which is produced through condensation of the universal C(5) isoprene units dimethylallyl diphosphate and isopentenyl diphosphate by prenyltransferases. We found that (+)-fusicocca-2,10 (14)-diene, a tricyclic hydrocarbon precursor for fusicoccins, is biosynthesized from the C(5) isoprene units by an unusual multifunctional enzyme, P. amygdali fusicoccadiene synthase (PaFS), which shows both prenyltransferase and terpene cyclase activities. The functional analysis of truncated mutants and site-directed mutagenesis demonstrated that PaFS consists of two domains: a terpene cyclase domain at the N terminus and a prenyltransferase domain at the C terminus. These findings suggest that fusicoccadiene can be produced efficiently in the fungus by using the C(5) precursors, irrespective of GGDP availability. In fact, heterologous expression of PaFS alone resulted in the accumulation of fusicocca-2,10 (14)-diene in Escherichia coli cells, whereas no product was detected in E. coli cells expressing Gibberella fujikuroi ent-kaurene synthase, another fungal diterpene cyclase that also uses GGDP as a substrate but does not contain a prenyltransferase domain. Genome walking suggested that fusicoccin biosynthetic enzymes are encoded as a gene cluster near the PaFS gene.

Indexed as

Base SequenceCloning, MolecularDNA PrimersEscherichia coliFungiGas Chromatography-Mass SpectrometryGlycosidesMolecular Sequence DataMutagenesis, Site-DirectedMycotoxinsPeptide SynthasesProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionSequence Analysis, DNADNA PrimersfusicoccinGlycosidesMycotoxinsPeptide Synthases

Identifiers

PMID17360612
PMCPMC1805559
OpenAlexW2030485246

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.