Evidence map›Paper›PMID 26117542›Full record

ArticleNucleic acids research2015

The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis.

Satyavati Kharde, Fabiola R Calviño, Andrea Gumiero, Klemens Wild, Irmgard Sinning

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 56 citations in OpenAlex.

  1. DCAF13 Safeguards Hematopoietic Stem Cells via RRS1-Regulated Ribosome Biogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

5 authors at 1 institution in 1 country.

Satyavati KhardeHeidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.
Fabiola R CalviñoHeidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.
Andrea GumieroHeidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.
Klemens WildHeidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.
Irmgard SinningHeidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany irmi.sinning@bzh.uni-heidelberg.de.
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly of eukaryotic ribosomes is a hierarchical process involving about 200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 and Rrs1 have been implicated in 5S RNP biogenesis, but their precise role was unclear. Here, we present the crystal structure of the Rpf2-Rrs1 complex from Aspergillus nidulans at 1.5 Å resolution and describe it as Brix domain of Rpf2 completed by Rrs1 to form two anticodon-binding domains with functionally important tails. Fitting the X-ray structure into the cryo-EM density of a previously described pre-60S particle correlates with biochemical data. The heterodimer forms specific contacts with the 5S rRNA, RpL5 and the biogenesis factor Rsa4. The flexible protein tails of Rpf2-Rrs1 localize to the central protuberance. Two helices in the Rrs1 C-terminal tail occupy a strategic position to block the rotation of 25S rRNA and the 5S RNP. Our data provide a structural model for 5S RNP recruitment to the pre-60S particle and explain why removal of Rpf2-Rrs1 is necessary for rearrangements to drive 60S maturation.

Indexed as

Aspergillus nidulansFungal ProteinsModels, MolecularProtein BindingProtein Structure, TertiaryRibonucleoproteinsRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsRNA, Ribosomal, 5SFungal ProteinsRibonucleoproteinsribosomal protein L11Ribosomal ProteinsRNA-Binding ProteinsRNA, Ribosomal, 5S

Identifiers

PMID26117542
PMCPMC4538828
OpenAlexW1581009165

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.