Evidence map›Paper›PMID 20716687›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Structural basis for the regulation of NtcA-dependent transcription by proteins PipX and PII.

José L Llácer, Javier Espinosa, Miguel A Castells, Asunción Contreras, Karl Forchhammer, Vicente Rubio

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

65 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. ModifiedMicroorganisms · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Allosteric regulation of nitrate transporter NRT via the signaling protein PII.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. DNA looping mediates cooperative transcription activation.Nature structural & molecular biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Transcriptional Regulation of the Creatine Utilization Genes ofFrontiers in bioengineering and biotechnology · 2022
    Article
  20. Article

5 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

6 authors at 4 institutions in 2 countries.

José L LlácerInstituto de Biomedicina de Valencia-Consejo Superior de Investigaciones Científicas, Centro de Investigación Biomédica en Red de Enfermedades Raras, Jaime Roig 11, Valencia 46010, Spain.
Javier Espinosa
Miguel A Castells
Asunción Contreras
Karl Forchhammer
Vicente Rubio
University of Alicante · ESUniversity of Tübingen · DECentro de Investigación Biomédica en Red · ESInstituto de Biomedicina de Valencia · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PII, an ancient and widespread signaling protein, transduces nitrogen/carbon/energy abundance signals through interactions with target proteins. We clarify structurally how PII regulates gene expression mediated by the transcription factor NtcA, the global nitrogen regulator of cyanobacteria, shedding light on NtcA structure and function and on how NtcA is activated by 2-oxoglutarate (2OG) and coactivated by the nonenzymatic PII target, protein PipX. We determine for the cyanobacteria Synechococcus elongatus the crystal structures of the PII-PipX and PipX-NtcA complexes and of NtcA in active and inactive conformations (respective resolutions, 3.2, 2.25, 2.3, and 3.05 A). The structures and the conclusions derived from them are consistent with the results of present and prior site-directed mutagenesis and functional studies. A tudor-like domain (TLD) makes up most of the PipX structure and mediates virtually all the contacts of PipX with PII and NtcA. In the PII-PipX complex, one PII trimer sequesters the TLDs of three PipX molecules between its body and its extended T loops, preventing PipX activation of NtcA. Changes in T loop conformation triggered by 2OG explain PII-PipX dissociation when 2OG is bound. The structure of active dimeric NtcA closely resembles that of the active cAMP receptor protein (CRP). This strongly suggests that with these proteins DNA binding, transcription activation, and allosteric regulation occur by common mechanisms, although the effectors are different. The PipX-NtcA complex consists of one active NtcA dimer and two PipX monomers. PipX coactivates NtcA by stabilizing its active conformation and by possibly helping recruit RNA polymerase but not by providing extra DNA contacts.

Indexed as

Bacterial ProteinsBinding SitesCrystallizationCrystallography, X-RayDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelKetoglutaric AcidsKineticsModels, MolecularMutagenesis, Site-DirectedMutationPII Nitrogen Regulatory ProteinsProtein BindingProtein ConformationProtein MultimerizationProtein Structure, TertiaryBacterial ProteinsDNA-Binding ProteinsKetoglutaric AcidsntcA protein, SynechococcusPII Nitrogen Regulatory ProteinsTranscription Factors

Identifiers

PMID20716687
PMCPMC2932567
OpenAlexW2106041483

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.