Evidence map›Paper›PMID 18948533›Full record

ArticleScience (New York, N.Y.)2008

The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation.

Kimberly J Durniak, Scott Bailey, Thomas A Steitz

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Review
  2. Computational redesign of a thermostable T7 RNA polymerase.Protein engineering, design & selection : PEDS · 2026
    Article
  3. Article
  4. Heterogeneous template-dependent transcription dynamics of T7 RNAP revealed by single-molecule imaging.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Computational redesign of a thermostable T7 RNA polymerase.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Understanding the impact ofFrontiers in molecular biosciences · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Structural basis of transition from initiation to elongation in de novo viral RNA-dependent RNA polymerases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

10 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.

Kimberly J DurniakDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.
Scott Bailey
Thomas A Steitz

Funding

STRUCTURES OF DNA POLYMERASES AND FUNCTIONAL COMPLEXESR01GM057510 · NIGMS · YALE UNIVERSITY · PI STEITZ, THOMAS ARTHUR · 1998 to 2013
$4.5M
NIGMS NIH HHS GM57510NIGMS NIH HHS R01 GM057510
6 · The paper itself

Abstract

Structural studies of the T7 bacteriophage DNA-dependent RNA polymerase (T7 RNAP) have shown that the conformation of the amino-terminal domain changes substantially between the initiation and elongation phases of transcription, but how this transition is achieved remains unclear. We report crystal structures of T7 RNAP bound to promoter DNA containing either a 7- or an 8-nucleotide (nt) RNA transcript that illuminate intermediate states along the transition pathway. The amino-terminal domain comprises the C-helix subdomain and the promoter binding domain (PBD), which consists of two segments separated by subdomain H. The structures of the intermediate complex reveal that the PBD and the bound promoter rotate by approximately 45 degrees upon synthesis of an 8-nt RNA transcript. This allows the promoter contacts to be maintained while the active site is expanded to accommodate a growing heteroduplex. The C-helix subdomain moves modestly toward its elongation conformation, whereas subdomain H remains in its initiation- rather than its elongation-phase location, more than 70 angstroms away.

Indexed as

Promoter Regions, GeneticTranscription, GeneticBacteriophage T7Crystallography, X-RayDNADNA-Directed RNA PolymerasesModels, GeneticModels, MolecularMutant ProteinsProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryViral Proteinsbacteriophage T7 RNA polymeraseDNADNA-Directed RNA PolymerasesMutant ProteinsViral Proteins

Identifiers

PMID18948533
PMCPMC2892258

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.