Evidence map›Paper›PMID 20511297›Full record

ArticleThe Plant cell2010

Plastidial thioredoxin z interacts with two fructokinase-like proteins in a thiol-dependent manner: evidence for an essential role in chloroplast development in Arabidopsis and Nicotiana benthamiana.

Borjana Arsova, Ursula Hoja, Matthias Wimmelbacher, Eva Greiner, Suayib Ustün, Michael Melzer, Kerstin Petersen, Wolfgang Lein, Frederik Börnke

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.

0numbers the graph read from it
0cells of the map it votes in
149citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

149 citing papers in PubMed, 328 citations in OpenAlex.

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89 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 1 country.

Borjana ArsovaMax-Planck Institute of Molecular Plant Physiology, Golm, Germany. arsova@mpimp-golm.mpg.de
Ursula Hoja
Matthias Wimmelbacher
Eva Greiner
Suayib Ustün
Michael Melzer
Kerstin Petersen
Wolfgang Lein
Frederik Börnke
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEMax Planck Society · DELeibniz Institute of Plant Genetics and Crop Plant Research · DEMax Planck Institute of Molecular Plant Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we characterize a plastidial thioredoxin (TRX) isoform from Arabidopsis thaliana that defines a previously unknown branch of plastidial TRXs lying between x- and y-type TRXs and thus was named TRX z. An Arabidopsis knockout mutant of TRX z had a severe albino phenotype and was inhibited in chloroplast development. Quantitative real-time RT-PCR analysis of the mutant suggested that the expressions of genes that depend on a plastid-encoded RNA polymerase (PEP) were specifically decreased. Similar results were obtained upon virus-induced gene silencing (VIGS) of the TRX z ortholog in Nicotiana benthamiana. We found that two fructokinase-like proteins (FLN1 and FLN2), members of the pfkB-carbohydrate kinase family, were potential TRX z target proteins and identified conserved Cys residues mediating the FLN-TRX z interaction. VIGS in N. benthamiana and inducible RNA interference in Arabidopsis of FLNs also led to a repression of PEP-dependent gene transcription. Remarkably, recombinant FLNs displayed no detectable sugar-phosphorylating activity, and amino acid substitutions within the predicted active site imply that the FLNs have acquired a new function, which might be regulatory rather than metabolic. We were able to show that the FLN2 redox state changes in vivo during light/dark transitions and that this change is mediated by TRX z. Taken together, our data strongly suggest an important role for TRX z and both FLNs in the regulation of PEP-dependent transcription in chloroplasts.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsCysteineDarknessFructokinasesGene Expression Regulation, PlantGene SilencingGenes, PlantMolecular Sequence DataNicotianaOxidation-ReductionPhenotypePhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein TransportArabidopsis ProteinsCysteineFLN1 protein, ArabidopsisFLN2 protein, ArabidopsisfructokinaseFructokinasesPhosphotransferases (Alcohol Group Acceptor)Recombinant ProteinsSulfhydryl CompoundsThioredoxins

Identifiers

PMID20511297
PMCPMC2899873
OpenAlexW2103600914

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.