Evidence map›Paper›PMID 22117216›Full record

ArticleThe EMBO journal2011

Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.

Shuang Li, Jingqi Duan, Dandan Li, Shoucai Ma, Keqiong Ye

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

43 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. SnoRNAs: Exploring Their Implication in Human Diseases.International journal of molecular sciences · 2024
    Review
  7. Clinical and translational medicine · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. HumanFrontiers in genetics · 2023
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  20. The cellular landscape of mid-size noncoding RNA.Wiley interdisciplinary reviews. RNA · 2019
    Review
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.

Shuang LiDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Beijing Normal University, Beijing, China.
Jingqi Duan
Dandan Li
Shoucai Ma
Keqiong Ye
National Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shq1 is a conserved protein required for the biogenesis of eukaryotic H/ACA ribonucleoproteins (RNPs), including human telomerase. We report the structure of the Shq1-specific domain alone and in complex with H/ACA RNP proteins Cbf5, Nop10 and Gar1. The Shq1-specific domain adopts a novel helical fold and primarily contacts the PUA domain and the otherwise disordered C-terminal extension (CTE) of Cbf5. The structure shows that dyskeratosis congenita mutations found in the CTE of human Cbf5 likely interfere with Shq1 binding. However, most mutations in the PUA domain are not located at the Shq1-binding surface and also have little effect on the yeast Cbf5-Shq1 interaction. Shq1 binds Cbf5 independently of the H/ACA RNP proteins Nop10, Gar1 and Nhp2 and the assembly factor Naf1, but shares an overlapping binding surface with H/ACA RNA. Shq1 point mutations that disrupt Cbf5 interaction suppress yeast growth particularly at elevated temperatures. Our results suggest that Shq1 functions as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA.

Indexed as

Amino Acid SequenceCrystallography, X-RayDyskeratosis CongenitaHumansHydro-LyasesMicrotubule-Associated ProteinsMolecular Sequence DataMutationNuclear ProteinsProtein ConformationRibonucleoproteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsCBF5 protein, S cerevisiaeGAR1 protein, S cerevisiaeHydro-LyasesMicrotubule-Associated ProteinsNOP10 protein, S cerevisiaeNuclear ProteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsShq1 protein, S cerevisiae

Identifiers

PMID22117216
PMCPMC3242979
OpenAlexW2110156957

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.