Evidence map›Paper›PMID 20876336›Full record

ArticleJournal of experimental botany2011

Thioredoxin-regulated beta-amylase (BAM1) triggers diurnal starch degradation in guard cells, and in mesophyll cells under osmotic stress.

Concetta Valerio, Alex Costa, Lucia Marri, Emmanuelle Issakidis-Bourguet, Paolo Pupillo, Paolo Trost, Francesca Sparla

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
10.3field-weighted citation impact, top 2% 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

90 citing papers in PubMed, 209 citations in OpenAlex.

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30 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

7 authors at 3 institutions in 2 countries.

Concetta ValerioDepartment of Experimental Evolutionary Biology, University of Bologna, Via Irnerio 42, I-40126 Bologna Italy.
Alex Costa
Lucia Marri
Emmanuelle Issakidis-Bourguet
Paolo Pupillo
Paolo Trost
Francesca Sparla
University of Bologna · ITUniversité Paris-Sud · FRUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BAM1 is a plastid-targeted β-amylase of Arabidopsis thaliana specifically activated by reducing conditions. Among eight different chloroplast thioredoxin isoforms, thioredoxin f1 was the most efficient redox mediator, followed by thioredoxins m1, m2, y1, y2, and m4. Plastid-localized NADPH-thioredoxin reductase (NTRC) was also able partially to restore the activity of oxidized BAM1. Promoter activity of BAM1 was studied by reporter gene expression (GUS and YFP) in Arabidopsis transgenic plants. In young (non-flowering) plants, BAM1 was expressed both in leaves and roots, but expression in leaves was mainly restricted to guard cells. Compared with wild-type plants, bam1 knockout mutants were characterized by having more starch in illuminated guard cells and reduced stomata opening, suggesting that thioredoxin-regulated BAM1 plays a role in diurnal starch degradation which sustains stomata opening. Besides guard cells, BAM1 appears in mesophyll cells of young plants as a result of a strongly induced gene expression under osmotic stress, which is paralleled by an increase in total β-amylase activity together with its redox-sensitive fraction. Osmotic stress impairs the rate of diurnal starch accumulation in leaves of wild-type plants, but has no effect on starch accumulation in bam1 mutants. It is proposed that thioredoxin-regulated BAM1 activates a starch degradation pathway in illuminated mesophyll cells upon osmotic stress, similar to the diurnal pathway of starch degradation in guard cells that is also dependent on thioredoxin-regulated BAM1.

Indexed as

Gene Expression Regulation, EnzymologicArabidopsisArabidopsis ProteinsChloroplast ThioredoxinsGene Expression Regulation, PlantOsmosisPlant LeavesPlant StomataProtein Serine-Threonine KinasesStarchStress, PhysiologicalThioredoxin-Disulfide ReductaseArabidopsis ProteinsBAM1 protein, ArabidopsisChloroplast ThioredoxinsProtein Serine-Threonine KinasesStarchThioredoxin-Disulfide Reductase

Identifiers

PMID20876336
PMCPMC3003804
OpenAlexW2169966075

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

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.