Evidence map›Paper›PMID 18757802›Full record

ArticleMicrobiology (Reading, England)2008

Identification and functional characterization of NifA variants that are independent of GlnB activation in the photosynthetic bacterium Rhodospirillum rubrum.

Xiaoxiao Zou, Yu Zhu, Edward L Pohlmann, Jilun Li, Yaoping Zhang, Gary P Roberts

Abstract read
In one paragraph

Article in Microbiology (Reading, England), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  6. Effect of point mutations on Herbaspirillum seropedicae NifA activity.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

6 authors at 2 institutions in 2 countries.

Xiaoxiao ZouDepartment of Microbiology and Immunology, College of Biological Sciences and State Key Laboratory for Agrobiotechnology, China Agricultural University, Beijing 100094, PR China.
Yu ZhuDepartment of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Edward L PohlmannDepartment of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Jilun LiDepartment of Microbiology and Immunology, College of Biological Sciences and State Key Laboratory for Agrobiotechnology, China Agricultural University, Beijing 100094, PR China.
Yaoping ZhangDepartment of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Gary P RobertsDepartment of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
University of Wisconsin–Madison · USChina Agricultural University · CN

Funding

PII: multiple homologs of a global regulatorR01GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2002 to 2011
$2.0M
Molecular basis of PII functionR56GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2007 to 2007
$203k
NIGMS NIH HHS GM65891NIGMS NIH HHS R01 GM065891NIGMS NIH HHS R56 GM065891
6 · The paper itself

Abstract

The activity of NifA, the transcriptional activator of the nitrogen fixation (nif) gene, is tightly regulated in response to ammonium and oxygen. However, the mechanisms for the regulation of NifA activity are quite different among various nitrogen-fixing bacteria. Unlike the well-studied NifL-NifA regulatory systems in Klebsiella pneumoniae and Azotobacter vinelandii, in Rhodospirillum rubrum NifA is activated by a direct protein-protein interaction with the uridylylated form of GlnB, which in turn causes a conformational change in NifA. We report the identification of several substitutions in the N-terminal GAF domain of R. rubrum NifA that allow NifA to be activated in the absence of GlnB. Presumably these substitutions cause conformational changes in NifA necessary for activation, without interaction with GlnB. We also found that wild-type NifA can be activated in a GlnB-independent manner under certain growth conditions, suggesting that some other effector(s) can also activate NifA. An attempt to use Tn5 mutagenesis to obtain mutants that altered the pool of these presumptive effector(s) failed, though much rarer spontaneous mutations in nifA were detected. This suggests that the necessary alteration of the pool of effector(s) for NifA activation cannot be obtained by knockout mutations.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsChromosomes, BacterialEscherichia coliGenes, BacterialGenes, RegulatorMutationNitrogenNitrogenaseNitrogen FixationPII Nitrogen Regulatory ProteinsPlasmidsRhodospirillum rubrumTranscription FactorsTwo-Hybrid System TechniquesBacterial ProteinsNifA protein, BacteriaNitrogenNitrogenasePIID regulatory protein, BacteriaPII Nitrogen Regulatory ProteinsTranscription Factors

Identifiers

PMID18757802
PMCPMC3484679
OpenAlexW2147453793

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.