Evidence map›Paper›PMID 28180304›Full record

ArticleNucleic acids research2017

RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.

Tatiana Mikhailova, Ekaterina Shuvalova, Alexander Ivanov, Denis Susorov, Alexey Shuvalov, Peter M Kolosov, Elena Alkalaeva

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
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  6. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
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  8. The mechanosensitive geneAmerican journal of physiology. Cell physiology · 2024
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  11. Gle1 is required for tRNA to stimulate Dbp5 ATPase activitybioRxiv : the preprint server for biology · 2023
    Article
  12. Article
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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

7 authors at 2 institutions in 1 country.

Tatiana MikhailovaEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Ekaterina ShuvalovaEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Alexander IvanovEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Denis SusorovEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Alexey ShuvalovEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Peter M KolosovEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Elena AlkalaevaEngelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Engelhardt Institute of Molecular Biology · RULomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human DEAD-box RNA-helicase DDX19 functions in mRNA export through the nuclear pore complex. The yeast homolog of this protein, Dbp5, has been reported to participate in translation termination. Using a reconstituted mammalian in vitro translation system, we show that the human protein DDX19 is also important for translation termination. It is associated with the fraction of translating ribosomes. We show that DDX19 interacts with pre-termination complexes (preTCs) in a nucleotide-dependent manner. Furthermore, DDX19 increases the efficiency of termination complex (TC) formation and the peptide release in the presence of eukaryotic release factors. Using the eRF1(AGQ) mutant protein or a non-hydrolysable analog of GTP to inhibit subsequent peptidyl-tRNA hydrolysis, we reveal that the activation of translation termination by DDX19 occurs during the stop codon recognition. This activation is a result of DDX19 binding to preTC and a concomitant stabilization of terminating ribosomes. Moreover, we show that DDX19 stabilizes ribosome complexes with translation elongation factors eEF1 and eEF2. Taken together, our findings reveal that the human RNA helicase DDX19 actively participates in protein biosynthesis.

Indexed as

Codon, TerminatorDEAD-box RNA HelicasesHEK293 CellsHumansMutationNucleocytoplasmic Transport ProteinsPeptide Chain Elongation, TranslationalPeptide Chain Termination, TranslationalPeptide Elongation Factor 1Peptide Elongation Factor 2PolyribosomesRibosomesRNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinsCodon, TerminatorDBP5 protein, S cerevisiaeDDX19B protein, humanDEAD-box RNA HelicasesNucleocytoplasmic Transport ProteinsPeptide Elongation Factor 1Peptide Elongation Factor 2RNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinstRNA, peptidyl-

Identifiers

PMID28180304
PMCPMC5605241
OpenAlexW2586235837

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

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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.