Evidence map›Paper›PMID 20600118›Full record

ArticleJournal of molecular biology2010

The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase.

Kook Sun Ha, Innokenti Toulokhonov, Dmitry G Vassylyev, Robert Landick

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

64 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. mBio · 2025
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Dynamic competition between a ligand and transcription factor NusA governs riboswitch-mediated transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021
    Review
  16. Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Review
  19. Mechanisms of Transcriptional Pausing in Bacteria.Journal of molecular biology · 2019
    Review
  20. Article

4 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

4 authors at 2 institutions in 1 country.

Kook Sun HaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Innokenti Toulokhonov
Dmitry G Vassylyev
Robert Landick
University of Wisconsin–Madison · USUniversity of Alabama at Birmingham · US

Funding

STRUCTURE/FUNCTION OF TRANSCRIPTION COMPLEX RNA HAIRPINSR01GM038660 · NIGMS · WASHINGTON UNIVERSITY · PI Robert Landick · 1992 to 2026
$12.2M
Structure/Function of Transcription Complex RNA HairpinsR37GM038660 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI LANDICK, ROBERT · 2001 to 2010
$5.5M
Transcription Regulation Through RNAP Secondary ChannelR01GM074840 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI VASSYLYEV, DMITRY G · 2005 to 2013
$4.1M
Molecular mechanisms of transcription elongationR01GM074252 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI VASSYLYEV, DMITRY G · 2005 to 2009
$2.4M
STRUCTURE/FUNCTION OF TRANSCRIPTION COMPLEX RNA HAIRPINSR29GM038660 · NIGMS · WASHINGTON UNIVERSITY · PI LANDICK, ROBERT · 1987 to 1991
–
NIGMS NIH HHS GM038660NIGMS NIH HHS GM074252NIGMS NIH HHS R01 GM038660NIGMS NIH HHS R01 GM074252NIGMS NIH HHS R01 GM074840NIGMS NIH HHS R37 GM038660
6 · The paper itself

Abstract

NusA is a core, multidomain regulator of transcript elongation in bacteria and archaea. Bacterial NusA interacts with elongating complexes and the nascent RNA transcript in ways that stimulate pausing and termination but that can be switched to antipausing and antitermination by other accessory proteins. This regulatory complexity of NusA likely depends on its multidomain structure, but it remains unclear which NusA domains possess which regulatory activity and how they interact with elongating RNA polymerase. We used a series of truncated NusA proteins to measure the effect of the NusA domains on transcriptional pausing and termination. We find that the N-terminal domain (NTD) of NusA is necessary and sufficient for enhancement of transcriptional pausing and that the other NusA domains contribute to NusA binding to elongating complexes. Stimulation of intrinsic termination requires higher concentrations of NusA and involves both the NTD and other NusA domains. Using a tethered chemical protease in addition to protein-RNA cross-linking, we show that the NusA NTD contacts the RNA exit channel of RNA polymerase. Finally, we report evidence that the NusA NTD recognizes duplex RNA in the RNA exit channel.

Indexed as

DNA-Directed RNA PolymerasesEscherichia coli ProteinsModels, MolecularNucleic Acid ConformationPeptide Elongation FactorsProtein ConformationRNA, BacterialTerminator Regions, GeneticTranscriptional Elongation FactorsTranscription FactorsTranscription, GeneticDNA-Directed RNA PolymerasesEscherichia coli ProteinsnusA protein, E coliPeptide Elongation FactorsRNA, BacterialTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID20600118
PMCPMC3682478
OpenAlexW2019028223

What OpenQuestion holds

Textmetadata
LicenceTDM
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.