Evidence map›Paper›PMID 17360376›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

S-adenosylmethionine directly inhibits binding of 30S ribosomal subunits to the SMK box translational riboswitch RNA.

Ryan T Fuchs, Frank J Grundy, Tina M Henkin

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Observation of preQRNA biology · 2019
    Article
  9. Article
  10. Article
  11. Review
  12. New tRNA contacts facilitate ligand binding in aProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Computational Methods for Modeling Aptamers and Designing Riboswitches.International journal of molecular sciences · 2017
    Review
  14. Review
  15. Article
  16. T box riboswitches in Actinobacteria: translational regulation via novel tRNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Review
  18. Dual-acting riboswitch control of translation initiation and mRNA decay.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Article
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 2 institutions in 2 countries.

Ryan T FuchsDepartment of Microbiology and RNA Group, Ohio State University, 484 West 12th Avenue, Columbus, OH 43210, USA.
Frank J Grundy
Tina M Henkin
Czech Academy of Sciences, Institute of Microbiology · CZThe Ohio State University · US

Funding

REGULATION OF METHIONINE METABOLISM IN BACILLUS SUBTILISR01GM063615 · NIGMS · OHIO STATE UNIVERSITY · PI HENKIN, TINA M. · 2001 to 2013
$3.7M
NIGMS NIH HHS GM63615NIGMS NIH HHS R01 GM063615
6 · The paper itself

Abstract

The S(MK) box is a conserved riboswitch motif found in the 5' untranslated region of metK genes [encoding S-adenosylmethionine (SAM) synthetase] in lactic acid bacteria, including Enterococcus, Streptococcus, and Lactococcus sp. Previous studies showed that this RNA element binds SAM in vitro, and SAM binding causes a structural rearrangement that sequesters the Shine-Dalgarno (SD) sequence by pairing with an anti-SD (ASD) element. A model was proposed in which SAM binding inhibits metK translation by preventing binding of the ribosome to the SD region of the mRNA. In the current work, the addition of SAM was shown to inhibit binding of 30S ribosomal subunits to S(MK) box RNA; in contrast, the addition of S-adenosylhomocysteine (SAH) had no effect. A mutant RNA, which has a disrupted SD-ASD pairing, was defective in SAM binding and showed no reduction of ribosome binding in the presence of SAM, whereas a compensatory mutation that restored SD-ASD pairing restored the response to SAM. Primer extension inhibition assays provided further evidence for SD-ASD pairing in the presence of SAM. These results strongly support the model that S(MK) box translational repression operates through occlusion of the ribosome binding site and that SAM binding requires the SD-ASD pairing.

Indexed as

Genes, BacterialProtein BiosynthesisBase SequenceDNA PrimersEnterococcus faecalisMolecular Sequence DataMutationNucleic Acid ConformationRegulatory Sequences, Nucleic AcidRibosomesRNA, BacterialS-AdenosylmethionineDNA PrimersRNA, BacterialS-Adenosylmethionine

Identifiers

PMID17360376
PMCPMC1829232
OpenAlexW1969229800

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.