Evidence map›Paper›PMID 33793899›Full record

ArticlePlant physiology2021

Alternative splicing creates a pseudo-strictosidine β-d-glucosidase modulating alkaloid synthesis in Catharanthus roseus.

Inês Carqueijeiro, Konstantinos Koudounas, Thomas Dugé de Bernonville, Liuda Johana Sepúlveda, Angela Mosquera, Dikki Pedenla Bomzan, Audrey Oudin, Arnaud Lanoue, Sébastien Besseau, Pamela Lemos Cruz and 13 more

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Tuning reductase activity in monoterpene indole alkaloid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Critical parameters for robustPlant direct · 2024
    Article
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  15. Alternative Splicing and Its Roles in Plant Metabolism.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Article
  18. 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

23 authors at 5 institutions in 5 countries.

Inês CarqueijeiroEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Konstantinos KoudounasEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Thomas Dugé de BernonvilleEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Liuda Johana SepúlvedaEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Angela MosqueraEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Dikki Pedenla BomzanMolecular Plant Biology and Biotechnology Lab, CSIR-Central Institute of Medicinal and Aromatic Plants, Research Centre, Bengaluru 560065, India.
Audrey OudinEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Arnaud LanoueEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Sébastien BesseauEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Pamela Lemos CruzEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Natalja KulaginaEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Emily A StanderEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Sébastien EymieuxINSERM U1259, Plateforme IBiSA de Microscopie Electronique, Université de Tours, 37200 Tours, France.
Julien Burlaud-GaillardINSERM U1259, Plateforme IBiSA de Microscopie Electronique, Université de Tours, 37200 Tours, France.
Emmanuelle BlanchardINSERM U1259, Plateforme IBiSA de Microscopie Electronique, Université de Tours, 37200 Tours, France.
Marc ClastreEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Lucia AtehortùaLaboratorio de Biotecnología, Universidad de Antioquia, Sede de Investigación Universitaria, 50010 Medellin, Colombia.
Benoit St-PierreEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Nathalie Giglioli-Guivarc'hEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Nicolas PaponEA3142 "Groupe d'Etude des Interactions Hôte-Pathogène," Université d'Angers, 49035 Angers, France.
Dinesh A NagegowdaMolecular Plant Biology and Biotechnology Lab, CSIR-Central Institute of Medicinal and Aromatic Plants, Research Centre, Bengaluru 560065, India.
Sarah E O'ConnorDepartment of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany.
Vincent CourdavaultEA2106 "Biomolécules et Biotechnologies Végétales," Université de Tours, 37200 Tours, France.
Université de Tours · FRCentral Institute of Medicinal and Aromatic Plants · INInteractions hôtes-agents pathogènes · FRMax Planck Institute for Chemical Ecology · DEUniversidad de Antioquia · CO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deglycosylation is a key step in the activation of specialized metabolites involved in plant defense mechanisms. This reaction is notably catalyzed by β-glucosidases of the glycosyl hydrolase 1 (GH1) family such as strictosidine β-d-glucosidase (SGD) from Catharanthus roseus. SGD catalyzes the deglycosylation of strictosidine, forming a highly reactive aglycone involved in the synthesis of cytotoxic monoterpene indole alkaloids (MIAs) and in the crosslinking of aggressor proteins. By exploring C. roseus transcriptomic resources, we identified an alternative splicing event of the SGD gene leading to the formation of a shorter isoform of this enzyme (shSGD) that lacks the last 71-residues and whose transcript ratio with SGD ranges from 1.7% up to 42.8%, depending on organs and conditions. Whereas it completely lacks β-glucosidase activity, shSGD interacts with SGD and causes the disruption of SGD multimers. Such disorganization drastically inhibits SGD activity and impacts downstream MIA synthesis. In addition, shSGD disrupts the metabolic channeling of downstream biosynthetic steps by hampering the recruitment of tetrahydroalstonine synthase in cell nuclei. shSGD thus corresponds to a pseudo-enzyme acting as a regulator of MIA biosynthesis. These data shed light on a peculiar control mechanism of β-glucosidase multimerization, an organization common to many defensive GH1 members.

Indexed as

Alternative SplicingCatharanthusGene Expression Regulation, PlantPlant ProteinsVinca AlkaloidsPlant ProteinsstrictosidineVinca Alkaloids

Identifiers

PMID33793899
PMCPMC8133614
OpenAlexW3125329560

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.