Evidence map›Paper›PMID 24750273›Full record

ArticleMolecular microbiology2014

A conserved and essential basic region mediates tRNA binding to the Elp1 subunit of the Saccharomyces cerevisiae Elongator complex.

Rachael Di Santo, Susanne Bandau, Michael J R Stark

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. How Elongator Acetylates tRNA Bases.International journal of molecular sciences · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Structural insights into the function of Elongator.Cellular and molecular life sciences : CMLS · 2018
    Review
  10. Article
  11. Review
  12. Article
  13. Dimerization of elongator protein 1 is essential for Elongator complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Rachael Di SantoCentre for Gene Regulation & Expression, College of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, Scotland, UK.
Susanne Bandau
Michael J R Stark
University of Dundee · GB

Funding

Wellcome Trust 083524/Z/07/ZWellcome Trust 089690/Z/09/ZWellcome Trust 097945
6 · The paper itself

Abstract

Elongator is a conserved, multi-protein complex discovered in Saccharomyces cerevisiae, loss of which confers a range of pleiotropic phenotypes. Elongator in higher eukaryotes is required for normal growth and development and a mutation in the largest subunit of human Elongator (Elp1) causes familial dysautonomia, a severe recessive neuropathy. Elongator promotes addition of mcm(5) and ncm(5) modifications to uridine in the tRNA anticodon 'wobble' position in both yeast and higher eukaryotes. Since these modifications are required for the tRNAs to function efficiently, a translation defect caused by hypomodified tRNAs may therefore underlie the variety of phenotypes associated with Elongator dysfunction. The Elp1 carboxy-terminal domain contains a highly conserved arginine/lysine-rich region that resembles a nuclear localization sequence (NLS). Using alanine substitution mutagenesis, we show that this region is essential for Elongator's function in tRNA wobble uridine modification. However, rather than acting to determine the nucleo-cytoplasmic distribution of Elongator, we find that the basic region plays a critical role in a novel interaction between tRNA and the Elp1 carboxy-terminal domain. Thus the conserved basic region in Elp1 may be essential for tRNA wobble uridine modification by acting as tRNA binding motif.

Indexed as

DNA Mutational AnalysisHistone AcetyltransferasesMutagenesis, Site-DirectedMutation, MissensePeptide Elongation FactorsProtein BindingRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistone AcetyltransferasesIKI3 protein, S cerevisiaePeptide Elongation FactorsRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID24750273
PMCPMC4150532
OpenAlexW2142995923

What OpenQuestion holds

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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.