Evidence map›Paper›PMID 28115624›Full record

ArticleNucleic acids research2017

The G-patch protein NF-κB-repressing factor mediates the recruitment of the exonuclease XRN2 and activation of the RNA helicase DHX15 in human ribosome biogenesis.

Indira Memet, Carmen Doebele, Katherine E Sloan, Markus T Bohnsack

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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Downregulation of the mThe Journal of biological chemistry · 2024
    Article
  6. Unveiling the DHX15-G-patch interplay in retroviral RNA packaging.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The RNA methyltransferase METTL8 installs mNature communications · 2022
    Article
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Indira MemetInstitute for Molecular Biology, University Medical Center Göttingen, Georg-August-University, 37073 Göttingen, Germany.
Carmen DoebeleInstitute for Molecular Biology, University Medical Center Göttingen, Georg-August-University, 37073 Göttingen, Germany.
Katherine E SloanInstitute for Molecular Biology, University Medical Center Göttingen, Georg-August-University, 37073 Göttingen, Germany.
Markus T BohnsackInstitute for Molecular Biology, University Medical Center Göttingen, Georg-August-University, 37073 Göttingen, Germany.
Universitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the synthesis of ribosomal subunits, which involves the maturation of the ribosomal (r)RNAs and assembly of ribosomal proteins, requires the co-ordinated action of a plethora of ribosome biogenesis factors. Many of these cofactors remain to be characterized in human cells. Here, we demonstrate that the human G-patch protein NF-κB-repressing factor (NKRF) forms a pre-ribosomal subcomplex with the DEAH-box RNA helicase DHX15 and the 5΄-3΄ exonuclease XRN2. Using UV crosslinking and analysis of cDNA (CRAC), we reveal that NKRF binds to the transcribed spacer regions of the pre-rRNA transcript. Consistent with this, we find that depletion of NKRF, XRN2 or DHX15 impairs an early pre-rRNA cleavage step (A'). The catalytic activity of DHX15, which we demonstrate is stimulated by NKRF functioning as a cofactor, is required for efficient A' cleavage, suggesting that a structural remodelling event may facilitate processing at this site. In addition, we show that depletion of NKRF or XRN2 also leads to the accumulation of excised pre-rRNA spacer fragments and that NKRF is essential for recruitment of the exonuclease to nucleolar pre-ribosomal complexes. Our findings therefore reveal a novel pre-ribosomal subcomplex that plays distinct roles in the processing of pre-rRNAs and the turnover of excised spacer fragments.

Indexed as

Organelle BiogenesisBiocatalysisCell NucleolusEnzyme ActivationExoribonucleasesHEK293 CellsHeLa CellsHumansModels, BiologicalProtein BindingRepressor ProteinsRibosomesRibosome SubunitsRNA HelicasesRNA PrecursorsRNA Processing, Post-TranscriptionalDHX15 protein, humanExoribonucleasesNKRF protein, humanRepressor ProteinsRNA HelicasesRNA PrecursorsRNA, RibosomalXRN2 protein, human

Identifiers

PMID28115624
PMCPMC5435916
OpenAlexW2580614250

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.