Evidence map›Paper›PMID 20088902›Full record

ArticleThe Plant journal : for cell and molecular biology2010

AtSIG6, a plastid sigma factor from Arabidopsis, reveals functional impact of cpCK2 phosphorylation.

Jennifer Schweer, Hacer Türkeri, Brigitte Link, Gerhard Link

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  5. Plastid Gene Transcription: An Update on Promoters and RNA Polymerases.Methods in molecular biology (Clifton, N.J.) · 2021
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  19. Evolutionary rewiring: a modified prokaryotic gene-regulatory pathway in chloroplasts.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  20. Review
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

4 authors at 1 institution in 1 country.

Jennifer SchweerLaboratory of Plant Cell Physiology and Molecular Biology, University of Bochum, Universitaetsstr. 150, 44780 Bochum, Germany.
Hacer Türkeri
Brigitte Link
Gerhard Link
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plastids contain sigma factors, i.e. gene-regulatory proteins for promoter binding and transcription initiation. Despite the physical and functional similarity shared with their prokaryotic counterparts, the plant sigma factors have distinguishing features: most notably the existence of a variable extra sequence comprising their N-terminal portions. This distinct architecture is reflected by functional differences, including phosphorylation control by organellar protein kinase(s) closely related to nucleocytosolic, rather than bacterial-type, enzymes. In particular, cpCK2, a nuclear-coded plastid-targeted casein kinase 2, has been implicated as a key component in plant sigma factor phosphorylation and transcriptional regulation (Eur. J. Biochem. 269, 2002, 3329; Planta, 219, 2004, 298). Although this notion is based mainly on biochemical evidence and in vitro systems, the recent availability of Arabidopsis sigma knock-out lines for complementation by intact and mutant sigma cDNAs has opened up new strategies for the study of transcription regulatory mechanisms in vivo. Using Arabidopsis sigma factor 6 (AtSIG6) as a paradigm, we present data suggesting that: (i) this factor is a substrate for regulatory phosphorylation by cpCK2 both in vitro and in vivo; (ii) cpCK2 phosphorylation of SIG6 occurs at multiple sites, which can widely differ in their effect on the visual and/or molecular phenotype; (iii) in vivo usage of the perhaps most critical cpCK2 site defined by Ser174 requires (pre-)phosphorylation at the n + 3 serine residue Ser177, pointing to 'pathfinder' kinase activity capable of generating a functional cpCK2 substrate site.

Indexed as

Amino Acid MotifsArabidopsisArabidopsis ProteinsCasein Kinase IIChloroplastsGene Expression Regulation, PlantGene Knockout TechniquesMutagenesis, Site-DirectedPhosphorylationRecombinant ProteinsRNA, PlantSequence AlignmentSigma FactorArabidopsis ProteinsCasein Kinase IIRecombinant ProteinsRNA, PlantSIG6 protein, ArabidopsisSigma Factor

Identifiers

PMID20088902
PMCPMC2988416
OpenAlexW2158519884

What OpenQuestion holds

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LicenceCC BY
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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.