Evidence map›Paper›PMID 23485418›Full record

ArticleJournal of molecular biology2013

Nucleotides adjacent to the ligand-binding pocket are linked to activity tuning in the purine riboswitch.

Colby D Stoddard, Jeremy Widmann, Jeremiah J Trausch, Joan G Marcano-Velázquez, Rob Knight, Robert T Batey

Abstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Biomolecules · 2024
    Article
  4. Mechanism of Ligand Discrimination by theJournal of chemical information and modeling · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Article
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  15. Review
  16. Article
  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Colby D StoddardDepartment of Chemistry and Biochemistry, 596 UCB, University of Colorado, Boulder, CO 80309-0596, USA.
Jeremy Widmann
Jeremiah J Trausch
Joan G Marcano-Velázquez
Rob Knight
Robert T Batey

Funding

MOLECULAR BIOLOGYT32GM007135 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI KRAUTER, KENNETH S · 1985 to 2012
$5.7M
Basis of Gene Regulation by Purine-Binding mRNAsR01GM073850 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI BATEY, ROBERT T · 2005 to 2022
$4.8M
Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
Purchase of an Isothermal Titration CalorimeterS10RR026516 · NCRR · UNIVERSITY OF COLORADO · PI BATEY, ROBERT T · 2010 to 2010
$129k
Howard Hughes Medical InstituteNCRR NIH HHS 1S10-RR026516NCRR NIH HHS S10 RR026516NIGMS NIH HHS GM073850NIGMS NIH HHS R01 GM073850NIGMS NIH HHS T32 GM007135NIGMS NIH HHS T32 GM065103NIGMS NIH HHS T32-GM07135
6 · The paper itself

Abstract

Direct sensing of intracellular metabolite concentrations by riboswitch RNAs provides an economical and rapid means to maintain metabolic homeostasis. Since many organisms employ the same class of riboswitch to control different genes or transcription units, it is likely that functional variation exists in riboswitches such that activity is tuned to meet cellular needs. Using a bioinformatic approach, we have identified a region of the purine riboswitch aptamer domain that displays conservation patterns linked to riboswitch activity. Aptamer domain compositions within this region can be divided into nine classes that display a spectrum of activities. Naturally occurring compositions in this region favor rapid association rate constants and slow dissociation rate constants for ligand binding. Using X-ray crystallography and chemical probing, we demonstrate that both the free and bound states are influenced by the composition of this region and that modest sequence alterations have a dramatic impact on activity. The introduction of non-natural compositions result in the inability to regulate gene expression in vivo, suggesting that aptamer domain activity is highly plastic and thus readily tunable to meet cellular needs.

Indexed as

RiboswitchAptamers, NucleotideBacillus subtilisBase PairingBase SequenceBinding SitesConserved SequenceCrystallography, X-RayLigandsModels, MolecularNucleic Acid ConformationPhylogenyPurine NucleotidesRNA, BacterialAptamers, NucleotideLigandsPurine NucleotidesRiboswitchRNA, Bacterial

Identifiers

PMID23485418
PMCPMC3769107

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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.