Evidence map›Paper›PMID 21652641›Full record

ArticleNucleic acids research2011

Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination.

Jason R Stagno, Amanda S Altieri, Mikhail Bubunenko, Sergey G Tarasov, Jess Li, Donald L Court, R Andrew Byrd, Xinhua Ji

Abstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Ligand-Based Drug Design of Novel Antimicrobials againstInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Spatial organization of RNA polymerase and its relationship with transcription inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Bacterial Transcription as a Target for Antibacterial Drug Development.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  15. Article
  16. Review
  17. Article
  18. Solution structure of lysine-free (K0) ubiquitin.Protein science : a publication of the Protein Society · 2014
    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

8 authors.

Jason R StagnoMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Amanda S Altieri
Mikhail Bubunenko
Sergey G Tarasov
Jess Li
Donald L Court
R Andrew Byrd
Xinhua Ji

Funding

Biomolecular Structure and Mechanism, Structure-Based Drug DesignZIABC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2009 to 2024
$27.3M
Lambda Genetic Networks and Lambda Red-Mediated RecombinationZIABC010336 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI COURT, DONALD · 2009 to 2020
$18.9M
CCR Biophysics Resource CoreZICBC010965 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI TARASOV, SERGEY · 2009 to 2025
$10.5M
Intramural NIH HHSNCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

Processive transcription antitermination requires the assembly of the complete antitermination complex, which is initiated by the formation of the ternary NusB-NusE-BoxA RNA complex. We have elucidated the crystal structure of this complex, demonstrating that the BoxA RNA is composed of 8 nt that are recognized by the NusB-NusE heterodimer. Functional biologic and biophysical data support the structural observations and establish the relative significance of key protein-protein and protein-RNA interactions. Further crystallographic investigation of a NusB-NusE-dsRNA complex reveals a heretofore unobserved dsRNA binding site contiguous with the BoxA binding site. We propose that the observed dsRNA represents BoxB RNA, as both single-stranded BoxA and double-stranded BoxB components are present in the classical lambda antitermination site. Combining these data with known interactions amongst antitermination factors suggests a specific model for the assembly of the complete antitermination complex.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesEscherichia coli ProteinsGenetic Complementation TestModels, MolecularMolecular Sequence DataMutationPhenotypeProtein MultimerizationRibosomal ProteinsRNARNA-Binding ProteinsRNA, Double-StrandedTranscription FactorsTranscription, Geneticantiterminator proteins, BacteriaBacterial ProteinsEscherichia coli ProteinsNusB protein, E coliRibosomal Proteinsribosomal protein S10RNARNA-Binding ProteinsRNA, Double-StrandedTranscription Factors

Identifiers

PMID21652641
PMCPMC3177189

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.