Evidence map›Paper›PMID 17034622›Full record

ArticleBMC molecular biology2006

N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination.

Valery N Urakov, Igor A Valouev, Natalia V Kochneva-Pervukhova, Anna N Packeiser, Alexander Yu Vishnevsky, Oleg O Glebov, Vladimir N Smirnov, Michael D Ter-Avanesyan

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  4. Cryptic MHC class I-binding peptides are revealed by aminoglycoside-induced stop codon read-through into the 3' UTR.Proceedings of the National Academy of Sciences of the United States of America · 2014
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  6. Sex, prions, and plasmids in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2012
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  9. Suicidal [PSI+] is a lethal yeast prion.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.BioEssays : news and reviews in molecular, cellular and developmental biology · 2008
    Review
  12. Article
  13. Review
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  15. Article
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  18. 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

8 authors at 3 institutions in 2 countries.

Valery N UrakovInstitute of Experimental Cardiology, Cardiology Research Center, Moscow, 121552, Russia. urakov@cardio.ru
Igor A Valouev
Natalia V Kochneva-Pervukhova
Anna N Packeiser
Alexander Yu Vishnevsky
Oleg O Glebov
Vladimir N Smirnov
Michael D Ter-Avanesyan
Institute of Experimental Cardiology · RUInstitute of Bioorganic Chemistry · RUMRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTermination of translation in eukaryotes requires two release factors, eRF1, which recognizes all three nonsense codons and facilitates release of the nascent polypeptide chain, and eRF3 stimulating translation termination in a GTP-depended manner. eRF3 from different organisms possess a highly conservative C region (eRF3C), which is responsible for the function in translation termination, and almost always contain the N-terminal extension, which is inessential and vary both in structure and length. In the yeast Saccharomyces cerevisiae the N-terminal region of eRF3 is responsible for conversion of this protein into the aggregated and functionally inactive prion form.

resultsHere, we examined functional importance of the N-terminal region of a non-prion form of yeast eRF3. The screen for mutations which are lethal in combination with the SUP35-C allele encoding eRF3C revealed the sup45 mutations which alter the N-terminal domain of eRF1 and increase nonsense codon readthrough. However, further analysis showed that synthetic lethality was not caused by the increased levels of nonsense codon readthrough. Dominant mutations in SUP35-C were obtained and characterized, which remove its synthetic lethality with the identified sup45 mutations, thus indicating that synthetic lethality was not due to a disruption of interaction with proteins that bind to this eRF3 region.

conclusionThese and other data demonstrate that the N-terminal region of eRF3 is involved both in modulation of the efficiency of translation termination and functioning of the eRF1/eRF3 complex outside of translation termination.

Indexed as

AllelesCodon, TerminatorMutationPeptide Chain Termination, TranslationalPeptide Termination FactorsPrionsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionCodon, Terminatorpeptide-chain-release factor 3Peptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeSUP45 protein, S cerevisiae

Identifiers

PMID17034622
PMCPMC1617110
OpenAlexW2159577232

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.