Evidence map›Paper›PMID 26206671›Full record

ArticleNucleic acids research2015

Accurate placement of substrate RNA by Gar1 in H/ACA RNA-guided pseudouridylation.

Peng Wang, Lijiang Yang, Yi Qin Gao, Xin Sheng Zhao

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. 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

4 authors at 2 institutions in 1 country.

Peng WangCollege of Chemistry and Molecular Engineering, Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Biodynamic Optical Imaging Center (BIOPIC), Peking University, Beijing 100871, China.
Lijiang YangCollege of Chemistry and Molecular Engineering, Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Biodynamic Optical Imaging Center (BIOPIC), Peking University, Beijing 100871, China.
Yi Qin GaoCollege of Chemistry and Molecular Engineering, Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Biodynamic Optical Imaging Center (BIOPIC), Peking University, Beijing 100871, China gaoyq@pku.edu.cn.
Xin Sheng ZhaoCollege of Chemistry and Molecular Engineering, Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Biodynamic Optical Imaging Center (BIOPIC), Peking University, Beijing 100871, China zhaoxs@pku.edu.cn.
Peking University · CNBeijing National Laboratory for Molecular Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

H/ACA RNA-guided ribonucleoprotein particle (RNP), the most complicated RNA pseudouridylase so far known, uses H/ACA guide RNA for substrate capture and four proteins (Cbf5, Nop10, L7Ae and Gar1) for pseudouridylation. Although it was shown that Gar1 not only facilitates the product release, but also enhances the catalytic activity, the chemical role that Gar1 plays in this complicated machinery is largely unknown. Kinetics measurement on Pyrococcus furiosus RNPs at different temperatures making use of fluorescence anisotropy showed that Gar1 reduces the catalytic barrier through affecting the activation entropy instead of enthalpy. Site-directed mutagenesis combined with molecular dynamics simulations demonstrated that V149 in the thumb loop of Cbf5 is critical in placing the target uridine to the right position toward catalytic D85 of Cbf5. The enzyme elegantly aligns the position of uridine in the catalytic site with the help of Gar1. In addition, conversion of uridine to pseudouridine results in a rigid syn configuration of the target nucleotide in the active site and causes Gar1 to pull out the thumb. Both factors guarantee the efficient release of the product.

Indexed as

Archaeal ProteinsCatalytic DomainEntropyIntramolecular TransferasesMolecular Dynamics SimulationMutagenesis, Site-DirectedPseudouridinePyrococcus furiosusRibonucleoproteins, Small NucleolarRNARNA, Small NucleolarUridineArchaeal ProteinsIntramolecular TransferasesPseudouridinepseudouridine synthasesRibonucleoproteins, Small NucleolarRNARNA, Small NucleolarUridine

Identifiers

PMID26206671
PMCPMC4551948
OpenAlexW1932782362

What OpenQuestion holds

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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.