Evidence map›Paper›PMID 21857665›Full record

ArticleNature structural & molecular biology2011

The structural basis of RNA-catalyzed RNA polymerization.

David M Shechner, David P Bartel

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact, top 95% 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

24 citing papers in PubMed, 0 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cryo-EM structure and functional landscape of an RNA polymerase ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. A ribozyme that uses lanthanides as cofactor.Nucleic acids research · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. In vitro selection of ribozyme ligases that use prebiotically plausible 2-aminoimidazole-activated substrates.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Models of Replicator Proliferation Involving Differential Replicator Subunit Stability.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. The ribosome challenge to the RNA world.Journal of molecular evolution · 2015
    Review
  20. 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

2 authors at 2 institutions in 1 country.

David M ShechnerWhitehead Institute for Biomedical Research, Cambridge, Massachusetts, USA.
David P Bartel
Howard Hughes Medical Institute · USWhitehead Institute for Biomedical Research · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI DONG, ZIGANG · 2001 to 2011
$28.2M
RNA CONFORMATION AND CATALYSISR01GM061835 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BARTEL, DAVID P · 2000 to 2008
$2.5M
RNA Conformation and CatalysisR37GM061835 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BARTEL, DAVID P · 2011 to 2016
$2.3M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS GM061835NIGMS NIH HHS R01 GM061835NIGMS NIH HHS R37 GM061835
6 · The paper itself

Abstract

Early life presumably required polymerase ribozymes capable of replicating RNA. Known polymerase ribozymes best approximating such replicases use as their catalytic engine an RNA-ligase ribozyme originally selected from random RNA sequences. Here we report 3.15-Å crystal structures of this ligase trapped in catalytically viable preligation states, with the 3'-hydroxyl nucleophile positioned for in-line attack on the 5'-triphosphate. Guided by metal- and solvent-mediated interactions, the 5'-triphosphate hooks into the major groove of the adjoining RNA duplex in an unanticipated conformation. Two phosphates and the nucleophile jointly coordinate an active-site metal ion. Atomic mutagenesis experiments demonstrate that active-site nucleobase and hydroxyl groups also participate directly in catalysis, collectively playing a role that in proteinaceous polymerases is performed by a second metal ion. Thus artificial ribozymes can use complex catalytic strategies that differ markedly from those of analogous biological enzymes.

Indexed as

Catalytic DomainCrystallography, X-RayModels, MolecularNucleic Acid ConformationPolymerizationPolyphosphatesRNARNA, CatalyticStatic ElectricityPolyphosphatesRNARNA, Catalytictriphosphoric acid

Identifiers

PMID21857665
PMCPMC3169305
OpenAlexW1589907089

What OpenQuestion holds

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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.