Evidence map›Paper›PMID 27688619›Full record

ArticlePlant physiology2016

Class II Cytochrome P450 Reductase Governs the Biosynthesis of Alkaloids.

Claire Parage, Emilien Foureau, Franziska Kellner, Vincent Burlat, Samira Mahroug, Arnaud Lanoue, Thomas Dugé de Bernonville, Monica Arias Londono, Inês Carqueijeiro, Audrey Oudin and 9 more

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

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  4. Genome-based discovery of pachysiphine synthases in Tabernaemontana elegans.The Plant journal : for cell and molecular biology · 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

19 authors at 2 institutions in 3 countries.

Claire ParageUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).ORCID 0000-0001-6161-2690
Emilien FoureauUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Franziska KellnerUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).ORCID 0000-0002-3424-6776
Vincent BurlatUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Samira MahrougUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Arnaud LanoueUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Thomas Dugé de BernonvilleUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Monica Arias LondonoUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Inês CarqueijeiroUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).ORCID 0000-0001-9576-5556
Audrey OudinUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Sébastien BesseauUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Nicolas PaponUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Gaëlle GlévarecUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Lucia AtehortùaUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Nathalie Giglioli-Guivarc'hUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Benoit St-PierreUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).ORCID 0000-0002-9077-2949
Marc ClastreUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.).
Sarah E O'ConnorUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.); sarah.o'connor@jic.ac.uk vincent.courdavault@univ-tours.fr.
Vincent CourdavaultUniversité François-Rabelais de Tours, EA2106 Biomolécules et Biotechnologies Végétales, F-37200 Tours, France (C.P., E.F., S.M., A.L., T.D.d.B., M.A.L., I.C., A.O., S.B., G.G., N.G.-G., B.S.-P., M.C., V.C.); sarah.o'connor@jic.ac.uk vincent.courdavault@univ-tours.fr.ORCID 0000-0001-8902-4532
John Innes Centre · GBUniversité de Tours · FR

Funding

Biotechnology and Biological Sciences Research Council BB/J004561/1
6 · The paper itself

Abstract

Expansion of the biosynthesis of plant specialized metabolites notably results from the massive recruitment of cytochrome P450s that catalyze multiple types of conversion of biosynthetic intermediates. For catalysis, P450s require a two-electron transfer catalyzed by shared cytochrome P450 oxidoreductases (CPRs), making these auxiliary proteins an essential component of specialized metabolism. CPR isoforms usually group into two distinct classes with different proposed roles, namely involvement in primary and basal specialized metabolisms for class I and inducible specialized metabolism for class II. By studying the role of CPRs in the biosynthesis of monoterpene indole alkaloids, we provide compelling evidence of an operational specialization of CPR isoforms in Catharanthus roseus (Madagascar periwinkle). Global analyses of gene expression correlation combined with transcript localization in specific leaf tissues and gene-silencing experiments of both classes of CPR all point to the strict requirement of class II CPRs for monoterpene indole alkaloid biosynthesis with a minimal or null role of class I. Direct assays of interaction and reduction of P450s in vitro, however, showed that both classes of CPR performed equally well. Such high specialization of class II CPRs in planta highlights the evolutionary strategy that ensures an efficient reduction of P450s in specialized metabolism.

Indexed as

Biosynthetic PathwaysAlkaloidsBiocatalysisCatharanthusCotyledonEndoplasmic ReticulumGene Expression Regulation, PlantGene SilencingGenes, PlantIndole AlkaloidsNADPH-Ferrihemoprotein ReductasePlant LeavesProtein BindingRNA, MessengerSequence Analysis, ProteinSequence Homology, Amino AcidAlkaloidsIndole AlkaloidsNADPH-Ferrihemoprotein ReductaseRNA, Messenger

Identifiers

PMID27688619
PMCPMC5100751
OpenAlexW2527007224

What OpenQuestion holds

Textmetadata
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Registered trials

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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.