Evidence map›Paper›PMID 19635803›Full record

ArticleThe Journal of biological chemistry2009

Unraveling delta1-pyrroline-5-carboxylate-proline cycle in plants by uncoupled expression of proline oxidation enzymes.

Gad Miller, Arik Honig, Hanan Stein, Nobuhiro Suzuki, Ron Mittler, Aviah Zilberstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

92 citing papers in PubMed, 252 citations in OpenAlex.

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  8. Measurement of δMetabolites · 2025
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  10. The Proline Dehydrogenase GeneInternational journal of molecular sciences · 2025
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  11. Review
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  19. HAntioxidants (Basel, Switzerland) · 2022
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32 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

6 authors at 3 institutions in 2 countries.

Gad MillerDepartment of Plant Science, Tel Aviv University, Tel-Aviv 69978, Israel.
Arik Honig
Hanan Stein
Nobuhiro Suzuki
Ron Mittler
Aviah Zilberstein
Tel Aviv University · ILUniversity of Nevada, Reno · USHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The two-step oxidation of proline in all eukaryotes is performed at the inner mitochondrial membrane by the consecutive action of proline dehydrogenase (ProDH) that produces Delta(1)-pyrroline-5-carboxylate (P5C) and P5C dehydrogenase (P5CDH) that oxidizes P5C to glutamate. This catabolic route is down-regulated in plants during osmotic stress, allowing free Pro accumulation. We show here that overexpression of MsProDH in tobacco and Arabidopsis or impairment of P5C oxidation in the Arabidopsis p5cdh mutant did not change the cellular Pro to P5C ratio under ambient and osmotic stress conditions, indicating that P5C excess was reduced to Pro in a mitochondrial-cytosolic cycle. This cycle, involving ProDH and P5C reductase, exists in animal cells and now demonstrated in plants. As a part of the cycle, Pro oxidation by the ProDH-FAD complex delivers electrons to the electron transport chain. Hyperactivity of the cycle, e.g. when an excess of exogenous l-Pro is provided, generates mitochondrial reactive oxygen species (ROS) by delivering electrons to O(2), as demonstrated by the mitochondria-specific MitoSox staining of superoxide ions. Lack of P5CDH activity led to higher ROS production under dark and light conditions in the presence of Pro excess, as well as rendered plants hypersensitive to heat stress. Balancing mitochondrial ROS production during increased Pro oxidation is therefore critical for avoiding Pro-related toxic effects. Hence, normal oxidation of P5C to Glu by P5CDH is key to prevent P5C-Pro intensive cycling and avoid ROS production from electron run-off.

Indexed as

1-Pyrroline-5-Carboxylate DehydrogenaseArabidopsisArabidopsis ProteinsDroughtsGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGlutamic AcidHot TemperatureMedicago sativaMitochondriaMutationNicotianaOxidation-ReductionPlantsPlants, Genetically ModifiedProline1-Pyrroline-5-Carboxylate DehydrogenaseALDH12A1 protein, ArabidopsisArabidopsis Proteinsdelta-1-pyrroline-5-carboxylateGlutamic AcidProlineProline OxidasePyrrolesReactive Oxygen SpeciesSodium Chloride

Identifiers

PMID19635803
PMCPMC2785336
OpenAlexW2018318080

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.