Evidence map›Paper›PMID 20822574›Full record

ReviewQuarterly reviews of biophysics2010

The glmS ribozyme: use of a small molecule coenzyme by a gene-regulatory RNA.

Adrian R Ferré-D'Amaré

Abstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Pioneering role of RNA in the early evolution of life.Genetics and molecular biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Mechanisms of catalytic RNA molecules.Biochemical Society transactions · 2021
    Review
  12. Article
  13. Review
  14. Review
  15. Riboswitches and Translation Control.Cold Spring Harbor perspectives in biology · 2018
    Review
  16. Article
  17. Riboswitch diversity and distribution.RNA (New York, N.Y.) · 2017
    Article
  18. A divalent cation-dependent variant of theRNA (New York, N.Y.) · 2017
    Article
  19. Review
  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

1 author at 1 institution in 1 country.

Adrian R Ferré-D'AmaréHoward Hughes Medical Institute, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109-1024, USA. aferre@fhcrc.org
Cancer Research Center · US

Funding

RNA: Structure, Biophysics and PhysiologyZIAHL006102 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2011 to 2025
$14.6M
Structural Biology of RNAR01GM063576 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI FERRE-D'AMARE, ADRIAN · 2001 to 2009
$2.8M
MSC BLUE-3 AND MSC PURPLE-3 CONFOCAL X-RAY OPTICSS10RR015943 · NCRR · FRED HUTCHINSON CANCER RESEARCH CENTER · PI FERRE-D'AMARE, ADRIAN R. · 2001 to 2001
$119k
Howard Hughes Medical InstituteIntramural NIH HHS Z99 HL999999Intramural NIH HHS ZIA HL006102NCRR NIH HHS RR15943NIGMS NIH HHS GM63576NIGMS NIH HHS R01 GM063576
6 · The paper itself

Abstract

The glmS ribozyme is the first known example of a natural ribozyme that has evolved to require binding of an exogenous small molecule for activity. In Gram-positive bacteria, this RNA domain is part of the messenger RNA (mRNA) encoding the essential enzyme that synthesizes glucosamine-6-phosphate (GlcN6P). When present at physiologic concentration, this small molecule binds to the glmS ribozyme and uncovers a latent self-cleavage activity that ultimately leads to degradation of the mRNA. Biochemical and structural studies reveal that the RNA adopts a rigid fold stabilized by three pseudoknots and the packing of a peripheral domain against the ribozyme core. GlcN6P binding to this pre-organized RNA does not induce conformational changes; rather, the small molecule functions as a coenzyme, providing a catalytically essential amine group to the active site. The ribozyme is not a passive player, however. Active site functional groups are essential for catalysis, even in the presence of GlcN6P. In addition to being a superb experimental system with which to analyze how RNA catalysts can exploit small molecule coenzymes to broaden their chemical versatility, the presence of the glmS ribozyme in numerous pathogenic bacteria make this RNA an attractive target for the development of new antibiotics and antibacterial strategies.

Indexed as

Bacterial ProteinsBase SequenceBiocatalysisCoenzymesGlucosamineGlucose-6-PhosphateMolecular Sequence DataRiboswitchRNA, CatalyticBacterial ProteinsCoenzymesGlucosamineglucosamine 6-phosphateGlucose-6-PhosphateRiboswitchRNA, Catalytic

Identifiers

PMID20822574
PMCPMC3409577
OpenAlexW1987542480

What OpenQuestion holds

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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.