Evidence map›Paper›PMID 24703949›Full record

ArticleMolecular cell2014

Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection.

Yu-He Liang, Mathieu Lavoie, Marc-Andre Comeau, Sherif Abou Elela, Xinhua Ji

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Journal of virology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Study of the role of MgJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Dicer's Helicase Domain: A Meeting Place for Regulatory Proteins.Cold Spring Harbor symposia on quantitative biology · 2019
    Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Yu-He LiangBiomolecular Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Mathieu LavoieRNA Group/Groupe ARN, Département de microbiologie et d'infectiologie, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Marc-Andre ComeauRNA Group/Groupe ARN, Département de microbiologie et d'infectiologie, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Sherif Abou ElelaRNA Group/Groupe ARN, Département de microbiologie et d'infectiologie, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada. Electronic address: sherif.abou.elela@usherbrooke.ca.
Xinhua JiBiomolecular Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA. Electronic address: jix@mail.nih.gov.
Université de Sherbrooke · CANational Cancer Institute · US

Funding

Biomolecular Structure and Mechanism, Structure-Based Drug DesignZIABC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2009 to 2024
$27.3M
CIHRIntramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC010326
6 · The paper itself

Abstract

Ribonuclease III (RNase III) enzymes are a family of double-stranded RNA (dsRNA)-specific endoribonucleases required for RNA maturation and gene regulation. Prokaryotic RNase III enzymes have been well characterized, but how eukaryotic RNase IIIs work is less clear. Here, we describe the structure of the Saccharomyces cerevisiae RNase III (Rnt1p) postcleavage complex and explain why Rnt1p binds to RNA stems capped with an NGNN tetraloop. The structure shows specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain (dsRBD) and the guanine nucleotide in the second position of the loop. Strikingly, structural and biochemical analyses indicate that the dsRBD and N-terminal domains (NTDs) of Rnt1p function as two rulers that measure the distance between the tetraloop and the cleavage site. These findings provide a framework for understanding eukaryotic RNase IIIs.

Indexed as

Amino Acid SequenceCatalytic DomainCrystallography, X-RayHydrogen BondingModels, MolecularProtein BindingRibonuclease IIIRNA CleavageRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityRibonuclease IIIRNA, FungalRNT1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID24703949
PMCPMC4019767
OpenAlexW2084908837

What OpenQuestion holds

Textmetadata
LicenceTDM
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.