Evidence map›Paper›PMID 11790752›Full record

ArticleJournal of bacteriology2002

Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii.

Paul Rudnick, Christopher Kunz, Malkanthi K Gunatilaka, Eric R Hines, Christina Kennedy

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Structural insights into redox signal transduction mechanisms in the control of nitrogen fixation by the NifLA system.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Paul RudnickDepartment of Plant Pathology, The University of Arizona, Tucson, AZ 85721, USA.
Christopher Kunz
Malkanthi K Gunatilaka
Eric R Hines
Christina Kennedy
University of Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In several diazotrophic species of Proteobacteria, P(II) signal transduction proteins have been implicated in the regulation of nitrogen fixation in response to NH(4)(+) by several mechanisms. In Azotobacter vinelandii, expression of nifA, encoding the nif-specific activator, is constitutive, and thus, regulation of NifA activity by the flavoprotein NifL appears to be the primary level of nitrogen control. In vitro and genetic evidence suggests that the nitrogen response involves the P(II)-like GlnK protein and GlnD (uridylyltransferase/uridylyl-removing enzyme), which reversibly uridylylates GlnK in response to nitrogen limitation. Here, the roles of GlnK and GlnK-UMP in A. vinelandii were studied to determine whether the Nif (-) phenotype of glnD strains was due to an inability to modify GlnK, an effort previously hampered because glnK is an essential gene in this organism. A glnKY51F mutation, encoding an unuridylylatable form of the protein, was stable only in a strain in which glutamine synthetase activity is not inhibited by NH(4)(+), suggesting that GlnK-UMP is required to signal adenylyltransferase/adenylyl-removing enzyme-mediated deadenylylation. glnKY51F strains were significantly impaired for diazotrophic growth and expression of a nifH-lacZ fusion. NifL interacted with GlnK and GlnKY51F in a yeast two-hybrid system. Together, these data are consistent with those obtained from in vitro experiments (Little et al., EMBO J., 19:6041-6050, 2000) and support a model for regulation of NifA activity in which unmodified GlnK stimulates NifL inhibition and uridylylation of GlnK in response to nitrogen limitation prevents this function. This model is distinct from one proposed for the related bacterium Klebsiella pneumoniae, in which unmodified GlnK relieves NifL inhibition instead of stimulating it.

Indexed as

Adenosine MonophosphateAzotobacter vinelandiiBacterial ProteinsCarrier ProteinsGene Expression Regulation, BacterialGlutamate-Ammonia LigaseKlebsiella pneumoniaeNitrogen FixationNucleotidyltransferasesProtein BindingProtein Processing, Post-TranslationalSuppression, GeneticTranscription FactorsTwo-Hybrid System TechniquesUridine MonophosphateAdenosine MonophosphateBacterial ProteinsCarrier ProteinsGlnK protein, Azorhizobium caulinodansGlutamate-Ammonia LigaseNifA protein, BacterianifL protein, BacteriaNucleotidyltransferasesTranscription FactorsUridine Monophosphate

Identifiers

PMID11790752
PMCPMC139532
OpenAlexW2160311957

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.