Evidence map›Paper›PMID 25588944›Full record

ArticleThe EMBO journal2015

A Tetrahymena Hsp90 co-chaperone promotes siRNA loading by ATP-dependent and ATP-independent mechanisms.

Sophie L Woehrer, Lucia Aronica, Jan H Suhren, Clara Jana-Lui Busch, Tomoko Noto, Kazufumi Mochizuki

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Hsp70 and Hsp90 Elaborately Regulate RNAi Efficiency inInternational journal of molecular sciences · 2023
    Article
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  6. Article
  7. Review
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Messages on small RNA duplexes in plants.Journal of plant research · 2017
    Review
  16. Review
  17. Article
  18. Article
  19. 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 2 institutions in 1 country.

Sophie L WoehrerInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Lucia AronicaInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Jan H SuhrenInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Clara Jana-Lui BuschInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Tomoko NotoInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Kazufumi MochizukiInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria kazufumi.mochizuki@imba.oeaw.ac.at.
Institute of Molecular Biotechnology · ATAustrian Academy of Sciences · AT

Funding

Austrian Science Fund FWF F 4307Austrian Science Fund FWF P 26032European Research Council 204986
6 · The paper itself

Abstract

The loading of small interfering RNAs (siRNAs) and microRNAs into Argonaute proteins is enhanced by Hsp90 and ATP in diverse eukaryotes. However, whether this loading also occurs independently of Hsp90 and ATP remains unclear. We show that the Tetrahymena Hsp90 co-chaperone Coi12p promotes siRNA loading into the Argonaute protein Twi1p in both ATP-dependent and ATP-independent manners in vitro. The ATP-dependent activity requires Hsp90 and the tetratricopeptide repeat (TPR) domain of Coi12p, whereas these factors are dispensable for the ATP-independent activity. Both activities facilitate siRNA loading by counteracting the Twi1p-binding protein Giw1p, which is important to specifically sort the 26- to 32-nt siRNAs to Twi1p. Although Coi12p lacking its TPR domain does not bind to Hsp90, it can partially restore the siRNA loading and DNA elimination defects of COI12 knockout cells, suggesting that Hsp90- and ATP-independent loading of siRNA occurs in vivo and plays a physiological role in Tetrahymena.

Indexed as

Argonaute ProteinsHSP90 Heat-Shock ProteinsMicroRNAsMolecular ChaperonesRNA, Small InterferingTetrahymenaArgonaute ProteinsHSP90 Heat-Shock ProteinsMicroRNAsMolecular ChaperonesRNA, Small InterferingArgonaute proteinRISC assemblyRNAisiRNATetrahymena

Identifiers

PMID25588944
PMCPMC4331008
OpenAlexW2156753527

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.