Evidence map›Paper›PMID 25855814›Full record

ArticleNucleic acids research2015

Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis.

Nozomi Asano, Koji Kato, Akiyoshi Nakamura, Keisuke Komoda, Isao Tanaka, Min Yao

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 44 citations in OpenAlex.

  1. DCAF13 Safeguards Hematopoietic Stem Cells via RRS1-Regulated Ribosome Biogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. World journal of gastrointestinal oncology · 2025
    Article
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  15. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  16. 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

6 authors at 1 institution in 1 country.

Nozomi AsanoGraduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Koji KatoGraduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Akiyoshi NakamuraFaculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Keisuke KomodaGraduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Isao TanakaFaculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Min YaoGraduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan yao@castor.sci.hokudai.ac.jp.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins Rpf2 and Rrs1 are required for 60S ribosomal subunit maturation. These proteins are necessary for the recruitment of three ribosomal components (5S ribosomal RNA [rRNA], RpL5 and RpL11) to the 90S ribosome precursor and subsequent 27SB pre-rRNA processing. Here we present the crystal structure of the Aspergillus nidulans (An) Rpf2-Rrs1 core complex. The core complex contains the tightly interlocked N-terminal domains of Rpf2 and Rrs1. The Rpf2 N-terminal domain includes a Brix domain characterized by similar N- and C-terminal architecture. The long α-helix of Rrs1 joins the C-terminal half of the Brix domain as if it were part of a single molecule. The conserved proline-rich linker connecting the N- and C-terminal domains of Rrs1 wrap around the side of Rpf2 and anchor the C-terminal domain of Rrs1 to a specific site on Rpf2. In addition, gel shift analysis revealed that the Rpf2-Rrs1 complex binds directly to 5S rRNA. Further analysis of Rpf2-Rrs1 mutants demonstrated that Saccharomyces cerevisiae Rpf2 R236 (corresponds to R238 of AnRpf2) plays a significant role in this binding. Based on these studies and previous reports, we have proposed a model for ribosomal component recruitment to the 90S ribosome precursor.

Indexed as

Aspergillus nidulansFungal ProteinsModels, MolecularProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationRibosomal ProteinsRibosomesRNA, Ribosomal, 5SFungal ProteinsRibosomal ProteinsRNA, Ribosomal, 5S

Identifiers

PMID25855814
PMCPMC4482071
OpenAlexW2069653972

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.