Evidence map›Paper›PMID 31732748›Full record

ArticleNucleic acids research2020

Structural transitions in the RNA 7SK 5' hairpin and their effect on HEXIM binding.

Konstantin Röder, Guillaume Stirnemann, Anne-Catherine Dock-Bregeon, David J Wales, Samuela Pasquali

Abstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Progress in 7SK ribonucleoprotein structural biology.Frontiers in molecular biosciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. An alternative D. melanogaster 7SK snRNP.BMC molecular and cell biology · 2021
    Article
  17. Article
  18. RNA Modeling with the Computational Energy Landscape Framework.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  19. 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

5 authors.

Konstantin RöderDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Guillaume StirnemannCNRS Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, PSL University, Université de Paris, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Anne-Catherine Dock-BregeonLaboratoire de Biologie Intégrative des Modèles Marins, UMR CNRS 8227, Sorbonne Université, Station Biologique de Roscoff, 29680 Roscoff, France.
David J WalesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Samuela PasqualiLaboratoire CiTCoM, CNRS UMR 8038, Université de Paris, 4 Avenue de l'observatoire, 75270 Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

7SK RNA, as part of the 7SK ribonucleoprotein complex, is crucial to the regulation of transcription by RNA-polymerase II, via its interaction with the positive transcription elongation factor P-TEFb. The interaction is induced by binding of the protein HEXIM to the 5' hairpin (HP1) of 7SK RNA. Four distinct structural models have been obtained experimentally for HP1. Here, we employ computational methods to investigate the relative stability of these structures, transitions between them, and the effects of mutations on the observed structural ensembles. We further analyse the results with respect to mutational binding assays, and hypothesize a mechanism for HEXIM binding. Our results indicate that the dominant structure in the wild type exhibits a triplet involving the unpaired nucleotide U40 and the base pair A43-U66 in the GAUC/GAUC repeat. This conformation leads to an open major groove with enough potential binding sites for peptide recognition. Sequence mutations of the RNA change the relative stability of the different structural ensembles. Binding affinity is consequently lost if these changes alter the dominant structure.

Indexed as

Transcription, GeneticBinding SitesHumansMolecular Dynamics SimulationNucleic Acid ConformationNucleotide MotifsPeptidesPositive Transcriptional Elongation Factor BProtein BindingRibonucleoproteinsRNA-Binding ProteinsRNA Polymerase IIRNA, Small CytoplasmicThermodynamicsTranscription FactorsHEXIM1 protein, humanPeptidesPositive Transcriptional Elongation Factor BRibonucleoproteinsRNA-Binding ProteinsRNA Polymerase IIRNA, Small CytoplasmicTranscription Factors

Identifiers

PMID31732748
PMCPMC7145557

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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.