Evidence map›Paper›PMID 19535331›Full record

ArticleThe Journal of biological chemistry2009

Structure, function, and targets of the transcriptional regulator SvtR from the hyperthermophilic archaeal virus SIRV1.

Florence Guillière, Nuno Peixeiro, Alexandra Kessler, Bertrand Raynal, Nicole Desnoues, Jenny Keller, Muriel Delepierre, David Prangishvili, Guennadi Sezonov, J Iñaki Guijarro

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Structure and mechanisms of viral transcription factors in archaea.Extremophiles : life under extreme conditions · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Archaeal extrachromosomal genetic elements.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  11. Article
  12. Host and viral transcriptional regulators in Sulfolobus: an overview.Extremophiles : life under extreme conditions · 2013
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. 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

10 authors at 4 institutions in 1 country.

Florence GuillièreInstitut Pasteur, Unité de RMN des Biomolécules, CNRS URA 2185, 75015 Paris.
Nuno PeixeiroInstitut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, 75015 Paris.
Alexandra KesslerInstitut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, 75015 Paris.
Bertrand RaynalInstitut Pasteur, Plate-forme de Biophysique des Macromolécules et de leurs Interactions, 75015 Paris.
Nicole DesnouesInstitut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, 75015 Paris.
Jenny KellerInstitut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS-UMR 8619, Université Paris 11, IFR115, Bâtiment 430, 91405 Orsay.
Muriel DelepierreInstitut Pasteur, Unité de RMN des Biomolécules, CNRS URA 2185, 75015 Paris.
David PrangishviliInstitut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, 75015 Paris.
Guennadi SezonovInstitut Pasteur, Unité de Biologie Moléculaire du Gène chez les Extrêmophiles, 75015 Paris; Université Pierre et Marie Curie, 4 place Jussieu, 75005 Paris, France.
J Iñaki GuijarroInstitut Pasteur, Unité de RMN des Biomolécules, CNRS URA 2185, 75015 Paris.
Institut Pasteur · FRLaboratoire des Biomolécules · FRBiology of Extremophiles Laboratory · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have characterized the structure and the function of the 6.6-kDa protein SvtR (formerly called gp08) from the rod-shaped virus SIRV1, which infects the hyperthermophilic archaeon Sulfolobus islandicus that thrives at 85 degrees C in hot acidic springs. The protein forms a dimer in solution. The NMR solution structure of the protein consists of a ribbon-helix-helix (RHH) fold between residues 13 and 56 and a disordered N-terminal region (residues 1-12). The structure is very similar to that of bacterial RHH proteins despite the low sequence similarity. We demonstrated that the protein binds DNA and uses its beta-sheet face for the interaction like bacterial RHH proteins. To detect all the binding sites on the 32.3-kb SIRV1 linear genome, we designed and performed a global genome-wide search of targets based on a simplified electrophoretic mobility shift assay. Four targets were recognized by the protein. The strongest binding was observed with the promoter of the gene coding for a virion structural protein. When assayed in a host reconstituted in vitro transcription system, the protein SvtR (Sulfolobus virus transcription regulator) repressed transcription from the latter promoter, as well as from the promoter of its own gene.

Indexed as

Gene Expression Regulation, ViralTranscription, GeneticBase SequenceBinding SitesCloning, MolecularDimerizationMolecular ConformationMolecular Sequence DataPromoter Regions, GeneticProtein BindingProtein Structure, SecondaryRudiviridaeStructure-Activity RelationshipSulfolobusViral ProteinsViral Proteins

Identifiers

PMID19535331
PMCPMC2755947
OpenAlexW2029523750

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.