Evidence map›Paper›PMID 19061645›Full record

ArticleMolecular cell2008

Structural basis for DNA-hairpin promoter recognition by the bacteriophage N4 virion RNA polymerase.

Michael L Gleghorn, Elena K Davydova, Lucia B Rothman-Denes, Katsuhiko S Murakami

Abstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021
    Article
  6. Article
  7. Global Proteomic Profiling ofJournal of virology · 2019
    Article
  8. Article
  9. A DNA structural alphabet provides new insight into DNA flexibility.Acta crystallographica. Section D, Structural biology · 2018
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Structure of Escherichia coli RNA polymerase holoenzyme at last.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Review
  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

4 authors.

Michael L GleghornDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Elena K Davydova
Lucia B Rothman-Denes
Katsuhiko S Murakami

Funding

Transcribing Activities in N4 Infected E. ColiR01AI012575 · NIAID · UNIVERSITY OF CHICAGO · PI ROTHMAN-DENES, LUCIA B. B · 1985 to 2013
$7.0M
X-Ray Crystallographic Studies of N4 RNA PolymerasesR01GM071897 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI MURAKAMI, KATSUHIKO · 2004 to 2008
$1.1M
NIAID NIH HHS AI12575NIAID NIH HHS R01 AI012575NIGMS NIH HHS GM071897NIGMS NIH HHS R01 GM071897
6 · The paper itself

Abstract

Coliphage N4 virion-encapsidated RNA polymerase (vRNAP) is a member of the phage T7-like single-subunit RNA polymerase (RNAP) family. Its central domain (mini-vRNAP) contains all RNAP functions of the full-length vRNAP, which recognizes a 5 to 7 base pair stem and 3 nucleotide loop hairpin DNA promoter. Here, we report the X-ray crystal structures of mini-vRNAP bound to promoters. Mini-vRNAP uses four structural motifs to recognize DNA sequences at the hairpin loop and stem and to unwind DNA. Despite their low sequence similarity, three out of four motifs are shared with T7 RNAP that recognizes a double-stranded DNA promoter. The binary complex structure and results of engineered disulfide linkage experiments reveal that the plug and motif B loop, which block the access of template DNA to the active site in the apo-form mini-vRNAP, undergo a large-scale conformational change upon promoter binding, explaining the restricted promoter specificity that is critical for N4 phage early transcription.

Indexed as

Nucleic Acid ConformationApoenzymesArginineBacteriophage N4Base PairingBase SequenceCatalytic DomainCrystallography, X-RayDNADNA-Directed RNA PolymerasesEnzyme ActivationModels, MolecularMolecular Sequence DataPromoter Regions, GeneticProtein Structure, SecondaryTranscription, GeneticApoenzymesArgininebacteriophage T7 RNA polymeraseDNADNA-Directed RNA PolymerasesViral Proteins

Identifiers

PMID19061645
PMCPMC2639713

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Registered trials

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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.