Evidence map›Paper›PMID 12198166›Full record

ArticleThe EMBO journal2002

Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities.

Thomas Steiner, Jens T Kaiser, Snezan Marinkoviç, Robert Huber, Markus C Wahl

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
2.1field-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

67 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
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  7. Article
  8. Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021
    Review
  9. Article
  10. 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
  11. Article
  12. Review
  13. Review
  14. The PFrontiers in molecular biosciences · 2018
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.Protein science : a publication of the Protein Society · 2016
    Article

7 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

5 authors at 1 institution in 1 country.

Thomas SteinerMax-Planck Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
Jens T Kaiser
Snezan Marinkoviç
Robert Huber
Markus C Wahl
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial transcription modulator NusG interacts with RNA polymerase and termination factor rho, displaying striking functional homology to eukaryotic Spt5. The protein is also a translational regulator. We have determined crystal structures of Aquifex aeolicus NusG showing a modular design: an N-terminal RNP-like domain, a C-terminal element with a KOW sequence motif and a species-specific immunoglobulin-like fold. The structures reveal bona fide nucleic acid binding sites, and nucleic acid binding activities can be detected for NusG from three organisms and for the KOW element alone. A conserved KOW domain is defined as a new class of nucleic acid binding folds. This module is a close structural homolog of tudor protein-protein interaction motifs. Putative protein binding sites for the RNP and KOW domains can be deduced, which differ from the areas implicated in nucleic acid interactions. The results strongly argue that both protein and nucleic acid contacts are important for NusG's functions and that the factor can act as an adaptor mediating indirect protein-nucleic acid associations.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsModels, MolecularMolecular Sequence DataPeptide Elongation FactorsPoint MutationProtein BindingProtein ConformationProtein Structure, TertiaryRibosomesRNA, BacterialBacterial ProteinsDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsNusG protein, E coliPeptide Elongation FactorsRNA, BacterialRNA-Binding ProteinsTranscription Factors

Identifiers

PMID12198166
PMCPMC126194
OpenAlexW2094602426

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.