Evidence map›Paper›PMID 16484375›Full record

ArticleRNA (New York, N.Y.)2006

Characteristics of the glmS ribozyme suggest only structural roles for divalent metal ions.

Adam Roth, Ali Nahvi, Mark Lee, Inbal Jona, Ronald R Breaker

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Gas-sensing riboceptors.RNA biology · 2024
    Article
  6. Article
  7. Thoughts on how to think (and talk) about RNA structure.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Self-cleavage of theProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Ionic Strength Sensing in Living Cells.ACS chemical biology · 2017
    Article
  13. Article
  14. Review
  15. Article
  16. A divalent cation-dependent variant of theRNA (New York, N.Y.) · 2017
    Article
  17. Assessing the Potential Effects of Active Site MgThe journal of physical chemistry letters · 2016
    Article
  18. Article
  19. Chemistry and Biology of Self-Cleaving Ribozymes.Trends in biochemical sciences · 2015
    Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Adam RothHoward Hughes Medical Institute, Department of Molecular, Cellular and Developmental Biology, Yale University, P. O. Box 208103, New Haven, Connecticut 06520-8103, USA.
Ali Nahvi
Mark Lee
Inbal Jona
Ronald R Breaker
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glmS ribozyme is a riboswitch class that occurs in certain Gram-positive bacteria, where it resides within mRNAs encoding glucosamine 6-phosphate synthase. Members of this self-cleaving ribozyme class rapidly catalyze RNA transesterification upon binding GlcN6P, and genetic evidence suggests that this cleavage event is important for down-regulating GlmS protein expression. In this report, we present a refined secondary structure model of the glmS ribozyme and determine the importance of a conserved pseudoknot structure for optimal ribozyme function. Analyses of deletion constructs demonstrate that the pseudoknot, together with other structural elements, permits the ribozyme to achieve maximum rate constants for RNA cleavage at physiologically relevant Mg2+ concentrations. In addition, we show that substantial rate enhancements are supported by an exchange-inert cobalt (III) complex and by molar concentrations of monovalent ions. Our findings indicate that the glmS ribozyme forms a complex structure to employ catalytic strategies that do not require the direct participation of divalent metal ions.

Indexed as

Cations, DivalentBacillus cereusBacillus subtilisBacterial ProteinsBase SequenceGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)KineticsMetalsMolecular Sequence DataNucleic Acid ConformationRNA, BacterialSequence Homology, Nucleic AcidBacterial ProteinsCations, Divalentcomponent S, glutamate mutase protein, BacteriaGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)MetalsRNA, Bacterial

Identifiers

PMID16484375
PMCPMC1421096
OpenAlexW2035955641

What OpenQuestion holds

Textmetadata
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.