Evidence map›Paper›PMID 20630870›Full record

ArticleThe Journal of biological chemistry2010

Structural and functional insights into Saccharomyces cerevisiae Tpa1, a putative prolylhydroxylase influencing translation termination and transcription.

Julien Henri, Delphine Rispal, Emilie Bayart, Herman van Tilbeurgh, Bertrand Séraphin, Marc Graille

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Fungal morphogenesis.Cold Spring Harbor perspectives in medicine · 2014
    Review
  15. Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

6 authors at 4 institutions in 1 country.

Julien HenriInstitut de Biochimie et Biophysique Moléculaire et Cellulaire, CNRS UMR8619 Bat 430 Université Paris Sud, 91405 Orsay Cedex, France.
Delphine Rispal
Emilie Bayart
Herman van Tilbeurgh
Bertrand Séraphin
Marc Graille
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FRInstitut de Biochimie et Biophysique Moléculaire et Cellulaire · FRInstitut de génétique et de biologie moléculaire et cellulaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficiency of translation termination relies on the specific recognition of the three stop codons by the eukaryotic translation termination factor eRF1. To date only a few proteins are known to be involved in translation termination in eukaryotes. Saccharomyces cerevisiae Tpa1, a largely conserved but uncharacterized protein, has been described to associate with a messenger ribonucleoprotein complex located at the 3' end of mRNAs that contains at least eRF1, eRF3, and Pab1. Deletion of the TPA1 gene results in a decrease of translation termination efficacy and an increase in mRNAs half-lives and longer mRNA poly(A) tails. In parallel, Schizosaccharomyces pombe Ofd1, a Tpa1 ortholog, and its partner Nro1 have been implicated in the regulation of the stability of a transcription factor that regulates genes essential for the cell response to hypoxia. To gain insight into Tpa1/Ofd1 function, we have solved the crystal structure of S. cerevisiae Tpa1 protein. This protein is composed of two equivalent domains with the double-stranded β-helix fold. The N-terminal domain displays a highly conserved active site with strong similarities with prolyl-4-hydroxylases. Further functional studies show that the integrity of Tpa1 active site as well as the presence of Yor051c/Ett1 (the S. cerevisiae Nro1 ortholog) are essential for correct translation termination. In parallel, we show that Tpa1 represses the expression of genes regulated by Hap1, a transcription factor involved in the response to levels of heme and oxygen. Altogether, our results support that Tpa1 is a putative enzyme acting as an oxygen sensor and influencing several distinct regulatory pathways.

Indexed as

Protein FoldingCarrier ProteinsCatalytic DomainCrystallography, X-RayDNA-Binding ProteinsGene Expression Regulation, FungalHemeOxygenPeptide Chain Termination, TranslationalProcollagen-Proline DioxygenaseProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipTranscription FactorsTranscription, GeneticCarrier ProteinsDNA-Binding ProteinsHAP1 protein, S cerevisiaeHemeOxygenProcollagen-Proline DioxygenaseSaccharomyces cerevisiae ProteinsTpa1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID20630870
PMCPMC2945571
OpenAlexW1963697709

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.