Evidence map›Paper›PMID 17594112›Full record

ArticlePlanta2007

Both caffeoyl Coenzyme A 3-O-methyltransferase 1 and caffeic acid O-methyltransferase 1 are involved in redundant functions for lignin, flavonoids and sinapoyl malate biosynthesis in Arabidopsis.

Cao-Trung Do, Brigitte Pollet, Johanne Thévenin, Richard Sibout, Dominique Denoue, Yves Barrière, Catherine Lapierre, Lise Jouanin

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

138 citing papers in PubMed, 321 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Genome-Wide Analysis of the Caffeoyl Coenzyme A-O-Methyltransferase (International journal of molecular sciences · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Genome-wide analysis of the COMT gene family inFrontiers in plant science · 2025
    Article
  11. Article
  12. Article
  13. Plant terrestrialization: an environmental pull on the evolution of multi-sourced streptophyte phenolics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Identification of the Key GeneInternational journal of molecular sciences · 2024
    Article
  19. International journal of molecular sciences · 2024
    Article
  20. Article

78 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 6 institutions in 3 countries.

Cao-Trung DoBiologie Cellulaire, INRA, 78026, Versailles cedex, France.
Brigitte Pollet
Johanne Thévenin
Richard Sibout
Dominique Denoue
Yves Barrière
Catherine Lapierre
Lise Jouanin
Laboratoire de Génétique Cellulaire · FRBiologie et Gestion des Risques en Agriculture · FRCentre Intégré de Santé et de Services Sociaux des Laurentides · CADépartement Biologie et Amélioration des Plantes · FRInstitut National de la Recherche Agronomique · MAParisTech · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two methylation steps are necessary for the biosynthesis of monolignols, the lignin precursors. Caffeic acid O-methyltransferase (COMT) O-methylates at the C5 position of the phenolic ring. COMT is responsible for the biosynthesis of sinapyl alcohol, the precursor of syringyl lignin units. The O-methylation at the C3 position of the phenolic ring involves the Caffeoyl CoA 3-O-methyltransferase (CCoAOMT). The CCoAOMT 1 gene (At4g34050) is believed to encode the enzyme responsible for the first O-methylation in Arabidopsis thaliana. A CCoAOMT1 promoter-GUS fusion and immunolocalization experiments revealed that this gene is strongly and exclusively expressed in the vascular tissues of stems and roots. An Arabidopsis T-DNA null mutant named ccomt 1 was identified and characterised. The mutant stems are slightly smaller than wild-type stems in short-day growth conditions and has collapsed xylem elements. The lignin content of the stem is low and the S/G ratio is high mainly due to fewer G units. These results suggest that this O-methyltransferase is involved in G-unit biosynthesis but does not act alone to perform this step in monolignol biosynthesis. To determine which O-methyltransferase assists CCoAOMT 1, a comt 1 ccomt1 double mutant was generated and studied. The development of comt 1 ccomt1 is arrested at the plantlet stage in our growth conditions. Lignins of these plantlets are mainly composed of p-hydroxyphenyl units. Moreover, the double mutant does not synthesize sinapoyl malate, a soluble phenolic. These results suggest that CCoAOMT 1 and COMT 1 act together to methylate the C3 position of the phenolic ring of monolignols in Arabidopsis. In addition, they are both involved in the formation of sinapoyl malate and isorhamnetin.

Indexed as

ArabidopsisBase SequenceDNA PrimersFlavonoidsLigninMalatesMethyltransferasesPhenylpropionatesSpectroscopy, Fourier Transform Infrared2-O-sinapoylmalatecaffeate O-methyltransferasecaffeoyl-CoA O-methyltransferaseDNA PrimersFlavonoidsLigninMalatesMethyltransferasesPhenylpropionates

Identifiers

PMID17594112
OpenAlexW2041927889

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.