Evidence map›Paper›PMID 25569479›Full record

ArticlePLoS genetics2015

Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

Wael Abdel-Fattah, Daniel Jablonowski, Rachael Di Santo, Kathrin L Thüring, Viktor Scheidt, Alexander Hammermeister, Sara Ten Have, Mark Helm, Raffael Schaffrath, Michael J R Stark

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Yeast geneMicrobial cell (Graz, Austria) · 2023
    Article
  7. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  8. Article
  9. Article
  10. How Elongator Acetylates tRNA Bases.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

10 authors at 4 institutions in 2 countries.

Wael Abdel-FattahCentre for Gene Regulation & Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom; Institut für Biologie, FG Mikrobiologie, Universität Kassel, Germany.
Daniel JablonowskiInstitut für Biologie, FG Mikrobiologie, Universität Kassel, Germany.
Rachael Di SantoCentre for Gene Regulation & Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom.
Kathrin L ThüringInstitut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Germany.
Viktor ScheidtInstitut für Biologie, FG Mikrobiologie, Universität Kassel, Germany.
Alexander HammermeisterInstitut für Biologie, FG Mikrobiologie, Universität Kassel, Germany.
Sara Ten HaveCentre for Gene Regulation & Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom.
Mark HelmInstitut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Germany.
Raffael SchaffrathInstitut für Biologie, FG Mikrobiologie, Universität Kassel, Germany; Department of Genetics, University of Leicester, Leicester, United Kingdom.
Michael J R StarkCentre for Gene Regulation & Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom.
University of Kassel · DEUniversity of Dundee · GBJohannes Gutenberg University Mainz · DEUniversity of Leicester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F019106/1Biotechnology and Biological Sciences Research Council BB/F0191629/1Biotechnology and Biological Sciences Research Council BB/F019629/1Wellcome Trust 097945
6 · The paper itself

Abstract

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification function. Hrr25 protein kinase directly modifies Elp1 on two sites (Ser-1198 and Ser-1202) and through analyzing non-phosphorylatable (alanine) and acidic, phosphomimic substitutions at Ser-1198, Ser-1202 and Ser-1209, we provide evidence that phosphorylation plays a positive role in the tRNA modification function of Elongator and may regulate the interaction of Elongator both with its accessory protein Kti12 and with Hrr25 kinase.

Indexed as

Adaptor Proteins, Signal TransducingAlanineCasein Kinase IGene Expression Regulation, FungalHistone AcetyltransferasesMultiprotein ComplexesPeptide Elongation FactorsPhenotypePhosphorylationRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUridineAdaptor Proteins, Signal TransducingAlanineCasein Kinase IHistone AcetyltransferasesHRR25 protein, S cerevisiaeIKI3 protein, S cerevisiaeKTI12 protein, S cerevisiaeMultiprotein ComplexesPeptide Elongation FactorsRNA, TransferSaccharomyces cerevisiae ProteinsUridine

Identifiers

PMID25569479
PMCPMC4287497
OpenAlexW2320315757

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.