Evidence map›Paper›PMID 28082395›Full record

ArticleNucleic acids research2017

The crystal structure of the 5΄ functional domain of the transcription riboregulator 7SK.

Denise Martinez-Zapien, Pierre Legrand, Alastair G McEwen, Florence Proux, Tristan Cragnolini, Samuela Pasquali, Anne-Catherine Dock-Bregeon

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

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  6. Review
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  10. Progress in 7SK ribonucleoprotein structural biology.Frontiers in molecular biosciences · 2023
    Review
  11. Article
  12. Article
  13. Review
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  15. Article
  16. Review
  17. Article
  18. RNA Modeling with the Computational Energy Landscape Framework.Methods in molecular biology (Clifton, N.J.) · 2021
    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

7 authors at 2 institutions in 1 country.

Denise Martinez-ZapienBiotechnologie et signalisation cellulaire, CNRS UMR 7242, Ecole Supérieure de Biotechnologie de Strasbourg, F-67412 Illkirch, France.
Pierre LegrandSynchrotron SOLEIL, L'Orme des Merisiers, F-91190 Gif-sur-Yvette, France.
Alastair G McEwenInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.
Florence ProuxDepartment of functional genomics, CNRS UMR 8197, Institut de Biologie de l΄Ecole Normale Supérieure F-75005 Paris, France.
Tristan CragnoliniUniversity Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK.
Samuela PasqualiLaboratoire de Biochimie Théorique, IBPC, CNRS UPR 9080, Université Sorbonne Paris Cite, Paris Diderot, 75005 Paris, France.
Anne-Catherine Dock-BregeonDepartment of functional genomics, CNRS UMR 8197, Institut de Biologie de l΄Ecole Normale Supérieure F-75005 Paris, France.
Centre National de la Recherche Scientifique · FRSynchrotron soleil · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vertebrates, the 7SK RNA forms the scaffold of a complex, which regulates transcription pausing of RNA-polymerase II. By binding to the HEXIM protein, the complex comprising proteins LARP7 and MePCE captures the positive transcription elongation factor P-TEFb and prevents phosphorylation of pausing factors. The HEXIM-binding site embedded in the 5΄-hairpin of 7SK (HP1) encompasses a short signature sequence, a GAUC repeat framed by single-stranded uridines. The present crystal structure of HP1 shows a remarkably straight helical stack involving several unexpected triples formed at a central region. Surprisingly, two uridines of the signature sequence make triple interactions in the major groove of the (GAUC)2. The third uridine is turned outwards or inward, wedging between the other uridines, thus filling the major groove. A molecular dynamics simulation indicates that these two conformations of the signature sequence represent stable alternatives. Analyses of the interaction with the HEXIM protein confirm the importance of the triple interactions at the signature sequence. Altogether, the present structural analysis of 7SK HP1 highlights an original mechanism of swapping bases, which could represent a possible '7SK signature' and provides new insight into the functional importance of the plasticity of RNA.

Indexed as

Models, MolecularAdenineBinding SitesCrystallography, X-RayMolecular Dynamics SimulationMutationNucleic Acid ConformationRNA-Binding ProteinsRNA, Long NoncodingTranscription FactorsUridineAdenineHEXIM1 protein, humanlong non-coding RNA 7SK, humanRNA-Binding ProteinsRNA, Long NoncodingTranscription FactorsUridine

Identifiers

PMID28082395
PMCPMC5389472
OpenAlexW2575504731

What OpenQuestion holds

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LicenceCC BY-NC
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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.