Evidence map›Paper›PMID 24990943›Full record

ArticleThe Journal of biological chemistry2014

Interaction between ribosome assembly factors Krr1 and Faf1 is essential for formation of small ribosomal subunit in yeast.

Sanduo Zheng, Pengfei Lan, Ximing Liu, Keqiong Ye

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  9. Review
  10. Article
  11. The complete structure of the small-subunit processome.Nature structural & molecular biology · 2017
    Article
  12. Article
  13. Article
  14. Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017
    Article
  15. Article
  16. Article
  17. 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 2 institutions in 1 country.

Sanduo ZhengDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Beijing Normal University, Beijing 100875,; National Institute of Biological Sciences at Beijing, Beijing 102206, and.
Pengfei LanNational Institute of Biological Sciences at Beijing, Beijing 102206, and; Graduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730.
Ximing LiuNational Institute of Biological Sciences at Beijing, Beijing 102206, and.
Keqiong YeNational Institute of Biological Sciences at Beijing, Beijing 102206, and; Graduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100730,; Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. Electronic address: yekeqiong@nibs.ac.cn.
National Institute of Biological Sciences, Beijing · CNChinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome formation in Saccharomyces cerevisiae requires a large number of transiently associated assembly factors that coordinate processing and folding of pre-rRNA and binding of ribosomal proteins. Krr1 and Faf1 are two interacting proteins present in early 90 S precursor particles of the small ribosomal subunit. Here, we determined a co-crystal structure of the core domain of Krr1 bound to a 19-residue fragment of Faf1 at 2.8 Å resolution. The structure reveals that Krr1 consists of two packed K homology (KH) domains, KH1 and KH2, and resembles archaeal Dim2-like proteins. We show that KH1 is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1. KH2 contains a canonical RNA-binding surface and additionally associates with an α-helix of Faf1. Specific disruption of the Krr1-Faf1 interaction impaired early 18 S rRNA processing at sites A0, A1, and A2 and caused cell lethality, but it did not prevent incorporation of the two proteins into pre-ribosomes. The Krr1-Faf1 interaction likely maintains a critical conformation of 90 S pre-ribosomes required for pre-rRNA processing. Our results illustrate the versatility of KH domains in protein interaction and provide insight into the role of Krr1-Faf1 interaction in ribosome biogenesis.

Indexed as

Amino Acid MotifsCrystallography, X-RayProtein Structure, QuaternaryProtein Structure, TertiaryRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsRNA, FungalRNA Processing, Post-TranscriptionalRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFAF1 protein, S cerevisiaeKRR1 protein, S cerevisiaeRNA-Binding ProteinsRNA, FungalRNA, Ribosomal, 18SSaccharomyces cerevisiae ProteinsCrystal StructureProtein-Protein InteractionRibosome AssemblyRNA-binding ProteinrRNA Processing

Identifiers

PMID24990943
PMCPMC4132776
OpenAlexW2018635427

What OpenQuestion holds

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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.