Evidence map›Paper›PMID 19036836›Full record

ArticlePlant physiology2009

GS52 ecto-apyrase plays a critical role during soybean nodulation.

Manjula Govindarajulu, Sung-Yong Kim, Marc Libault, R Howard Berg, Kiwamu Tanaka, Gary Stacey, Christopher G Taylor

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
10.4field-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

31 citing papers in PubMed, 82 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Manjula GovindarajuluDonald Danforth Plant Science Center, St. Louis, Missouri 63132, USA.
Sung-Yong Kim
Marc Libault
R Howard Berg
Kiwamu Tanaka
Gary Stacey
Christopher G Taylor
University of Missouri · USDonald Danforth Plant Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apyrases are non-energy-coupled nucleotide phosphohydrolases that hydrolyze nucleoside triphosphates and nucleoside diphosphates to nucleoside monophosphates and orthophosphates. GS52, a soybean (Glycine soja) ecto-apyrase, was previously shown to be induced very early in response to inoculation with the symbiotic bacterium Bradyrhizobium japonicum. Overexpression of the GS52 ecto-apyrase in Lotus japonicus increased the level of rhizobial infection and enhanced nodulation. These data suggest a critical role for the GS52 ecto-apyrase during nodulation. To further investigate the role of GS52 during nodulation, we used RNA interference to silence GS52 expression in soybean (Glycine max) roots using Agrobacterium rhizogenes-mediated root transformation. Transcript levels of GS52 were significantly reduced in GS52 silenced roots and these roots exhibited reduced numbers of mature nodules. Development of the nodule primordium and subsequent nodule maturation was significantly suppressed in GS52 silenced roots. Transmission electron micrographs of GS52 silenced root nodules showed that early senescence and infected cortical cells were devoid of symbiosome-containing bacteroids. Application of exogenous adenosine diphosphate to silenced GS52 roots restored nodule development. Restored nodules contained bacteroids, thus indicating that extracellular adenosine diphosphate is important during nodulation. These results clearly suggest that GS52 ecto-apyrase catalytic activity is critical for the early B. japonicum infection process, initiation of nodule primordium development, and subsequent nodule organogenesis in soybean.

Indexed as

Adenosine DiphosphateAmino Acid SequenceApyraseGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGene SilencingGlycine maxMolecular Sequence DataNucleotidesPisum sativumPlant ProteinsPlant RootsPyrophosphatasesRNA InterferenceRNA, MessengerSolanum tuberosumAdenosine DiphosphateApyraseNucleotidesPlant ProteinsPyrophosphatasesRNA, Messenger

Identifiers

PMID19036836
PMCPMC2633840
OpenAlexW2057703795

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.