Evidence map›Paper›PMID 21383183›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation.

Damian Graczyk, Janusz Debski, Grazyna Muszyńska, Maria Bretner, Olivier Lefebvre, Magdalena Boguta

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

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  12. Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021
    Review
  13. Polymerase III transcription is necessary for T cell priming by dendritic cells.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Glycolytic flux inThe Biochemical journal · 2019
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Damian GraczykInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02 106 Warsaw, Poland.
Janusz Debski
Grazyna Muszyńska
Maria Bretner
Olivier Lefebvre
Magdalena Boguta
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLWarsaw University of Technology · PLCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maf1 protein is a global negative regulator of RNA polymerase (Pol) III transcription conserved from yeast to man. We report that phosphorylation of Maf1 by casein kinase II (CK2), a highly evolutionarily conserved eukaryotic kinase, is required for efficient Pol III transcription. Both recombinant human and yeast CK2 were able to phosphorylate purified human or yeast Maf1, indicating that Maf1 can be a direct substrate of CK2. Upon transfer of Saccharomyces cerevisiae from repressive to favorable growth conditions, CK2 activity is required for the release of Maf1 from Pol III bound to a tRNA gene and for subsequent activation of tRNA transcription. In a yeast strain lacking Maf1, CK2 inhibition showed no effect on tRNA synthesis, confirming that CK2 activates Pol III via Maf1. Additionally, CK2 was found to associate with tRNA genes, and this association is enhanced in absence of Maf1, especially under repressive conditions. These results corroborate the previously reported TFIIIB-CK2 interaction and indicate an important role of CK2-mediated Maf1 phosphorylation in triggering Pol III activation.

Indexed as

Casein Kinase IIEnzyme ActivationHumansPhosphorylationRepressor ProteinsRNA Polymerase IIIRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTranscription Factor TFIIIBTranscription, GeneticCasein Kinase IIMAF1 protein, humanMAF1 protein, S cerevisiaeRepressor ProteinsRNA Polymerase IIIRNA, TransferSaccharomyces cerevisiae ProteinsTranscription FactorsTranscription Factor TFIIIB

Identifiers

PMID21383183
PMCPMC3064340
OpenAlexW2116263238

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.