Evidence map›Paper›PMID 21087996›Full record

ArticleNucleic acids research2011

Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis.

Seth R Thomas, Christopher A Keller, Agnieszka Szyk, Joe R Cannon, Nicole A Laronde-Leblanc

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

46 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
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  6. Integrated Chemoenzymatic Synthesis of the mRNA Vaccine Building Block NAngewandte Chemie (International ed. in English) · 2025
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  7. Review
  8. Mechanisms of ribosomopathy and phase separation-related ribosomopathy.Journal of Zhejiang University. Science. B · 2025
    Review
  9. Article
  10. tRNA mbioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Review
  13. Article
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  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 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 3 institutions in 1 country.

Seth R ThomasDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.
Christopher A Keller
Agnieszka Szyk
Joe R Cannon
Nicole A Laronde-Leblanc
University of Maryland, Baltimore · USUniversity of Maryland, College Park · USUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI RAO, ANJANA · 2001 to 2011
$28.2M
NCRR NIH HHS RR-15301
6 · The paper itself

Abstract

Nucleolar Essential Protein 1 (Nep1) is required for small subunit (SSU) ribosomal RNA (rRNA) maturation and is mutated in Bowen-Conradi Syndrome. Although yeast (Saccharomyces cerevisiae) Nep1 interacts with a consensus sequence found in three regions of SSU rRNA, the molecular details of the interaction are unknown. Nep1 is a SPOUT RNA methyltransferase, and can catalyze methylation at the N1 of pseudouridine. Nep1 is also involved in assembly of Rps19, an SSU ribosomal protein. Mutations in Nep1 that result in decreased methyl donor binding do not result in lethality, suggesting that enzymatic activity may not be required for function, and RNA binding may play a more important role. To study these interactions, the crystal structures of the scNep1 dimer and its complexes with RNA were determined. The results demonstrate that Nep1 recognizes its RNA site via base-specific interactions and stabilizes a stem-loop in the bound RNA. Furthermore, the RNA structure observed contradicts the predicted structures of the Nep1-binding sites within mature rRNA, suggesting that the Nep1 changes rRNA structure upon binding. Finally, a uridine base is bound in the active site of Nep1, positioned for a methyltransfer at the C5 position, supporting its role as an N1-specific pseudouridine methyltransferase.

Indexed as

Amino Acid SequenceArchaeal ProteinsArchaeoglobus fulgidusCatalytic DomainDimerizationMethyltransferasesModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationPseudouridineRibosomal ProteinsRNARNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsArchaeal ProteinsEMG1 protein, S cerevisiaeMethyltransferasesPseudouridineRibosomal ProteinsRNARNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21087996
PMCPMC3064781
OpenAlexW2104107140

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.