Evidence map›Paper›PMID 31844059›Full record

ArticleNature communications2019

SAM-VI riboswitch structure and signature for ligand discrimination.

Aiai Sun, Catherina Gasser, Fudong Li, Hao Chen, Stefan Mair, Olga Krasheninina, Ronald Micura, Aiming Ren

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. A cooperative effect of ligands, MgThe Journal of biological chemistry · 2026
    Article
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  8. Riboswitch Mechanisms for Regulation of P1 Helix Stability.International journal of molecular sciences · 2024
    Review
  9. Biomolecules · 2024
    Article
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  13. Review
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  17. Probing RNA Structures and Interactions Using Fluorescence Lifetime Analyses.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Article
  19. Article
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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

8 authors at 3 institutions in 2 countries.

Aiai SunLife Sciences Institute, Zhejiang University, 310058, Hangzhou, Zhejiang, China.
Catherina GasserInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, A6020, Austria.
Fudong LiNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics and School of Life Sciences, University of Science and Technology of China, 230026, Hefei, China.
Hao ChenLife Sciences Institute, Zhejiang University, 310058, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0001-7436-5895
Stefan MairInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, A6020, Austria.
Olga KrashenininaInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, A6020, Austria.
Ronald MicuraInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, A6020, Austria. ronald.micura@uibk.ac.at.
Aiming RenLife Sciences Institute, Zhejiang University, 310058, Hangzhou, Zhejiang, China. aimingren@zju.edu.cn.ORCID http://orcid.org/0000-0002-5420-4899
Zhejiang University · CNUniversität Innsbruck · ATUniversity of Science and Technology of China · CN

Funding

Austrian Science Fund FWF M 2517Austrian Science Fund FWF P 27947Austrian Science Fund FWF P 31691
6 · The paper itself

Abstract

Riboswitches are metabolite-sensing, conserved domains located in non-coding regions of mRNA that are central to regulation of gene expression. Here we report the first three-dimensional structure of the recently discovered S-adenosyl-L-methionine responsive SAM-VI riboswitch. SAM-VI adopts a unique fold and ligand pocket that are distinct from all other known SAM riboswitch classes. The ligand binds to the junctional region with its adenine tightly intercalated and Hoogsteen base-paired. Furthermore, we reveal the ligand discrimination mode of SAM-VI by additional X-ray structures of this riboswitch bound to S-adenosyl-L-homocysteine and a synthetic ligand mimic, in combination with isothermal titration calorimetry and fluorescence spectroscopy to explore binding thermodynamics and kinetics. The structure is further evaluated by analysis of ligand binding to SAM-VI mutants. It thus provides a thorough basis for developing synthetic SAM cofactors for applications in chemical and synthetic RNA biology.

Indexed as

Models, MolecularNucleic Acid ConformationBifidobacteriumCrystallography, X-RayLigandsRiboswitchRNA, BacterialS-AdenosylmethionineLigandsRiboswitchRNA, BacterialS-Adenosylmethionine

Identifiers

PMID31844059
PMCPMC6914780
OpenAlexW2996195997

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.