Evidence map›Paper›PMID 19169240›Full record

ArticleNature2009

Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch.

Alexander Serganov, Lili Huang, Dinshaw J Patel

Abstract read
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed, 1 pooled it
8.1field-weighted citation impact, top 2% 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

154 citing papers in PubMed, 1 synthesis or guideline pooled it, 298 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Construction of antibiotic-free riboflavin producer inSynthetic and systems biotechnology · 2025
    Article
  13. Journal of chemical information and modeling · 2025
    Article
  14. Review
  15. Article
  16. TheRNA (New York, N.Y.) · 2024
    Article
  17. Review
  18. Riboswitch Mechanisms for Regulation of P1 Helix Stability.International journal of molecular sciences · 2024
    Review
  19. The current riboswitch landscape inMicrobiology (Reading, England) · 2024
    Review
  20. Review

94 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

3 authors at 1 institution in 1 country.

Alexander SerganovStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA. serganoa@mskcc.org
Lili Huang
Dinshaw J Patel
Memorial Sloan Kettering Cancer Center · US

Funding

RNA REGULATORY DOMAINS: FOLDING, RECOGNITION &CATALYSISR01GM073618 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI PATEL, DINSHAW J · 2005 to 2008
$1.3M
NIGMS NIH HHS R01 GM073618
6 · The paper itself

Abstract

The biosynthesis of several protein cofactors is subject to feedback regulation by riboswitches. Flavin mononucleotide (FMN)-specific riboswitches, also known as RFN elements, direct expression of bacterial genes involved in the biosynthesis and transport of riboflavin (vitamin B(2)) and related compounds. Here we present the crystal structures of the Fusobacterium nucleatum riboswitch bound to FMN, riboflavin and antibiotic roseoflavin. The FMN riboswitch structure, centred on an FMN-bound six-stem junction, does not fold by collinear stacking of adjacent helices, typical for folding of large RNAs. Rather, it adopts a butterfly-like scaffold, stapled together by opposingly directed but nearly identically folded peripheral domains. FMN is positioned asymmetrically within the junctional site and is specifically bound to RNA through interactions with the isoalloxazine ring chromophore and direct and Mg(2+)-mediated contacts with the phosphate moiety. Our structural data, complemented by binding and footprinting experiments, imply a largely pre-folded tertiary RNA architecture and FMN recognition mediated by conformational transitions within the junctional binding pocket. The inherent plasticity of the FMN-binding pocket and the availability of large openings make the riboswitch an attractive target for structure-based design of FMN-like antimicrobial compounds. Our studies also explain the effects of spontaneous and antibiotic-induced deregulatory mutations and provided molecular insights into FMN-based control of gene expression in normal and riboflavin-overproducing bacterial strains.

Indexed as

Gene Expression Regulation, BacterialCoenzymesFlavin MononucleotideFusobacterium nucleatumModels, MolecularNucleic Acid ConformationRNA, BacterialCoenzymesFlavin MononucleotideRNA, Bacterial

Identifiers

PMID19169240
PMCPMC3726715
OpenAlexW2159859043

What OpenQuestion holds

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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.