Evidence map›Paper›PMID 24087850›Full record

ArticleJournal of the American Chemical Society2013

Kinetics of allosteric transitions in S-adenosylmethionine riboswitch are accurately predicted from the folding landscape.

Jong-Chin Lin, D Thirumalai

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Incorporation of a FRET Pair into a Riboswitch RNA to Measure MgInternational journal of molecular sciences · 2022
    Article
  4. Article
  5. Computational Methods for Modeling Aptamers and Designing Riboswitches.International journal of molecular sciences · 2017
    Review
  6. Review
  7. Article
  8. Article
  9. Understanding the kinetic mechanism of RNA single base pair formation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Article
  12. Review
  13. Dynamics of riboswitches: Molecular simulations.Biochimica et biophysica acta · 2014
    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 1 institution in 1 country.

Jong-Chin LinDepartment of Chemistry and Biochemistry, Biophysics Program, Institute for Physical Sciences and Technology, University of Maryland , College Park, Maryland 20742, United States.
D Thirumalai
University of Maryland, College Park · US

Funding

Computational Approaches to Single Molecule Force SpectroscopyR01GM089685 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI THIRUMALAI, DEVARAJAN · 2010 to 2020
$2.9M
NIGMS NIH HHS GM 089685NIGMS NIH HHS R01 GM089685
6 · The paper itself

Abstract

Riboswitches are RNA elements that allosterically regulate gene expression by binding cellular metabolites. The SAM-III riboswitch, one of several classes that binds S-adenosylmethionine (SAM), represses translation upon binding SAM (OFF state) by encrypting the ribosome binding sequence. We have carried out simulations of the RNA by applying mechanical force (f) to the ends of SAM-III, with and without SAM, to get quantitative insights into the f-dependent structural changes. Force-extension (z) curves (FECs) for the apo (ON) state, obtained in simulations in which f is increased at a constant loading rate, show three intermediates, with the first one being the rupture of SAM binding region, which is greatly stabilized in the OFF state. Force-dependent free energy profiles, G(z,f), as a function of z, obtained in equilibrium constant force simulations, reveal the intermediates observed in FECs. The predicted stability difference between the ON and OFF states using G(z,f) is in excellent agreement with experiments. Remarkably, using G(z,f)s and estimate of an effective diffusion constant at a single value of f allows us to predict the f-dependent transition rates using theory of first passage times for both the apo and holo states. To resolve the kinetics of assembly of SAM-III riboswitch in structural terms, we use force stretch-quench pulse sequences in which the force on RNA is maintained at a low (fq) value starting from a high value for a time period tq. Variation of tq over a wide range results in resolution of elusive states involved in the SAM binding pocket and leads to accurate determination of folding times down to fq = 0. Quantitative measure of the folding kinetics, obtained from the folding landscape, allows us to propose that, in contrast to riboswitches regulating transcription, SAM-III functions under thermodynamic control provided the basal concentration of SAM exceeds a small critical value. All of the predictions are amenable to tests in single molecule pulling experiments.

Indexed as

RiboswitchAllosteric RegulationKineticsModels, MolecularProtein FoldingS-AdenosylmethionineRiboswitchS-Adenosylmethionine

Identifiers

PMID24087850
PMCPMC3861500
OpenAlexW2084501555

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.